Relevant bibliographies by topics / Human blood assay

Academic literature on the topic 'Human blood assay'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Human blood assay"

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Fedorov, N. A., I. S. Yaneva, O. I. Skotnikova, and V. N. Pan'kov. "DNA assay in human blood plasma." Bulletin of Experimental Biology and Medicine 102, no. 3 (September 1986): 1190–92. http://dx.doi.org/10.1007/bf00842228.

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Kaur, Satbir, Sangeeta Sangeeta, Kiranjeet Kaur Galhna, and Nisha Gautam. "Assessment of Radiation Induced DNA Damage in Human Peripheral Blood Lymphocytes Using COMET Assay." International Journal of Life- Sciences Scientific Research 3, no. 4 (July 6, 2017): 1208–14. http://dx.doi.org/10.21276/ijlssr.2017.3.4.17.

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Rosen, Steffen, Stefan Tiefenbacher, Mary Robinson, Mei Huang, Jaydeep Srimani, Donnie Mackenzie, Terri Christianson, et al. "Activity of transgene-produced B-domain–deleted factor VIII in human plasma following AAV5 gene therapy." Blood 136, no. 22 (November 26, 2020): 2524–34. http://dx.doi.org/10.1182/blood.2020005683.

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Abstract Adeno-associated virus (AAV)-based gene therapies can restore endogenous factor VIII (FVIII) expression in hemophilia A (HA). AAV vectors typically use a B-domain–deleted FVIII transgene, such as human FVIII-SQ in valoctocogene roxaparvovec (AAV5-FVIII-SQ). Surprisingly, the activity of transgene-produced FVIII-SQ was between 1.3 and 2.0 times higher in one-stage clot (OS) assays than in chromogenic-substrate (CS) assays, whereas recombinant FVIII-SQ products had lower OS than CS activity. Transgene-produced and recombinant FVIII-SQ showed comparable specific activity (international units per milligram) in the CS assay, demonstrating that the diverging activities arise in the OS assay. Higher OS activity for transgene-produced FVIII-SQ was observed across various assay kits and clinical laboratories, suggesting that intrinsic molecular features are potential root causes. Further experiments in 2 participants showed that transgene-produced FVIII-SQ accelerated early factor Xa and thrombin formation, which may explain the higher OS activity based on a kinetic bias between OS and CS assay readout times. Despite the faster onset of coagulation, global thrombin levels were unaffected. A correlation with joint bleeds suggested that both OS and CS assay remained clinically meaningful to distinguish hemophilic from nonhemophilic FVIII activity levels. During clinical development, the CS activity was chosen as a surrogate end point to conservatively assess hemostatic efficacy and enable comparison with recombinant FVIII-SQ products. Relevant trials are registered on clinicaltrials.gov as #NCT02576795 and #NCT03370913 and, respectively, on EudraCT (European Union Drug Regulating Authorities Clinical Trials Database; https://eudract.ema.europa.eu) as #2014-003880-38 and #2017-003215-19.
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Irie, Minoru, Yukitaka Miyachi, and Mari SEGAWA. "Measurement IGF-I in Human Blood by Immunoenzymometric Assay." Folia Endocrinologica Japonica 68, no. 7 (1992): 688–700. http://dx.doi.org/10.1507/endocrine1927.68.7_688.

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Fisher, T. C., J. J. F. Belch, J. C. Barbenel, and A. C. Fisher. "Human whole-blood granulocyte aggregation in vitro." Clinical Science 76, no. 2 (February 1, 1989): 183–87. http://dx.doi.org/10.1042/cs0760183.

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1. Aggregation assays are a commonly used technique for the study of granulocyte activation. These studies are usually performed using a pure cell suspension in buffer. This necessitates a separation procedure which is time-consuming and may modify the function of the cells. Interaction between different cell types is precluded. 2. To avoid these disadvantages a method was developed which quantifies granulocyte aggregation in whole blood. Samples drawn from an incubated vessel before and after the addition of a chemotactic stimulus were fixed with formaldehyde to prevent disaggregation. Erythrocytes were then removed by chemical lysis and using an electronic cell-sizing device the number of single cells and aggregates could then be easily measured. 3. Results from a group of volunteers showed a rapid and reversible response to a chemotactic tripeptide, with a fall in single granulocyte count and the appearance of doublets and triplets. Lymphocytes were unaffected. Intra-assay reproducibility was better than ± 5%. 4. Using this assay, a significant elevation in aggregability was observed in blood from patients after acute myocardial infarction. 5. This novel technique, by avoiding the separation step, is faster, simpler and more physiological than previous methods, and as such is useful for both assays of drug action in vitro and the study of cell activation in disease states.
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Russell, Bruce, Rossarin Suwanarusk, Céline Borlon, Fabio T. M. Costa, Cindy S. Chu, Marcus J. Rijken, Kanlaya Sriprawat, et al. "A reliable ex vivo invasion assay of human reticulocytes by Plasmodium vivax." Blood 118, no. 13 (September 29, 2011): e74-e81. http://dx.doi.org/10.1182/blood-2011-04-348748.

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AbstractCurrently, there are no reliable RBC invasion assays to guide the discovery of vaccines against Plasmodium vivax, the most prevalent malaria parasite in Asia and South America. Here we describe a protocol for an ex vivo P vivax invasion assay that can be easily deployed in laboratories located in endemic countries. The assay is based on mixing enriched cord blood reticulocytes with matured, trypsin-treated P vivax schizonts concentrated from clinical isolates. The reliability of this assay was demonstrated using a large panel of P vivax isolates freshly collected from patients in Thailand.
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Shinohara, Rikio, Yoshiji Ohta, Masamitsu Yamauchi, and Isao Ishiguro. "Improved fluorometric enzymatic sorbitol assay in human blood." Clinica Chimica Acta 273, no. 2 (May 1998): 171–84. http://dx.doi.org/10.1016/s0009-8981(98)00036-9.

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Wang, Xiaoying, Hao Li, Xiaoxi Li, Yangyang Chen, Yongmei Yin, and Genxi Li. "Electrochemical assay of melanoma biomarker in human blood." Electrochemistry Communications 39 (February 2014): 12–14. http://dx.doi.org/10.1016/j.elecom.2013.12.003.

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Modestino, Augusta, Matthew Tyndall, Johnson Yu, Roy B. Lefkowitz, Geert W. Schmid-Schönbein, and Michael J. Heller. "Thrombin generation assay in untreated whole human blood." ELECTROPHORESIS 37, no. 15-16 (August 2016): 2248–56. http://dx.doi.org/10.1002/elps.201600061.

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Kashyap, V. K. "A Simple Immunosorbent Assay for Detection of Human Blood." Journal of Immunoassay 10, no. 4 (December 1989): 315–24. http://dx.doi.org/10.1080/01971528908053244.

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Dissertations / Theses on the topic "Human blood assay"

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Kizilian, Narine. "Prediction of radiosensitivity by measurement of radiation-induced apoptosis in human blood using the comet assay." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0017/MQ48501.pdf.

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Kizilian, Narine Carleton University Dissertation Physics. "Prediction of radiosensitivity by measurement of radiation-induced apoptosis in human blood using the comet assay." Ottawa, 1999.

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Weir, Rosemary Edith. "Field studies of the human cell-mediated immune response to mycobacterium leprae using a whole blood assay." Thesis, London School of Hygiene and Tropical Medicine (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.264192.

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Osborn, Anna. "Measurements of Human Plasma Oxidation." Thesis, University of Canterbury. Biological Sciences, 2006. http://hdl.handle.net/10092/1426.

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The oxidation of lipids and antioxidants has been extensively studied in human plasma but little attention has been given to how plasma proteins are oxidised. Proteins make up the majority of biomolecules in cells and plasma and therefore are the most likely reactants with oxidants and free radicals. Previous studies in the laboratory had shown that peroxyl radicals generated by the thermolytic decay of 2-azobis (2-amdinopropane) dihydrochloride (AAPH) generated significant amounts of protein hydroperoxides, but only after a six hour lag period. In this study the existence of the six hour lag period was confirmed and shown by dialysis of the plasma to be due to the presence of low molecular weight antioxidants. The addition of both uric acid and ascorbic acid to the dialysed plasma restored the lag phase suggesting that in vivo these antioxidants act to prevent protein hydroperoxide formation. Lipid oxidation was also observed in the plasma but only after a two hour lag phase. This was the first time lipid oxidation has been observed in the absence of protein oxidation. The lipid lag phase was also abolished by dialysis of the plasma and restored by the addition of ascorbic acid and uric acid. The kinetics of tocopherol loss suggests that the tocopherol radicals act to inhibit lipid oxidation by transferring the electrons to the water-soluble ascorbate. The loss of ascorbate appears to cause the formation of a tocopherol radical mediate the lipid peroxidation process. Overall the data shows ascorbic acid scavenging the peroxyl radicals while uric acid acts to reduce the overall AAPH generated radical flux. In a separate investigation, the production of protein-bound DOPA (PB-DOPA) on albumin during X-ray radiolysis and copper mediate Fenton oxidation was investigated using a fluorescence based derivatisation method (ED-DOPA), which was compared with the more specific acid hydrolysis and HPLC analysis method. The ED-DOPA method consistently gave a much higher reading that the HPLC based methods, suggesting that the ED-DOPA method was measuring DOPA plus DOPA oxidation products. This was confirmed by oxidising X-ray radiolysis generated PB-DOPA with Cu++ to cause DOPA oxidation. The Cu++ treatment drastically increased the level of signal given by the ED-DOPA assay while HPLC analysis showed all the DOPA had been oxidised.
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Zekarias, Mikaela. "Characterization of rituximab-induced B cell depletion and infusion reactions in a human blood loop system." Thesis, Uppsala universitet, Institutionen för farmaceutisk biovetenskap, 2020. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-414582.

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Introduction: Rituximab is a monoclonal antibody used to treat hematological malignancies. The antibody depletes CD20+ B cells via cytotoxic immune mechanisms, such as complement-dependent cytotoxicity (CDC) and antibody-dependent cell-mediated cytotoxicity (ADCC), which is mainly induced by natural killer (NK) cells. Rituximab is mostly well-tolerated but has been reported to induce the release of large amounts of cytokines in blood, thus causing systemic inflammatory response. Aim: To study rituximab-induced B cell depletion and cytokine release in blood from healthy volunteers and how this was affected by Fc modified versions of the antibody. Methods and materials: Fresh blood from healthy donors (n=3) was incubated with rituximab and Fc modified versions that influence the antibody’s target functions, namely ADCC and CDC, for 4 hours in a blood loop system. Results were measured using multicolor flow cytometry, except for cytokine release in plasma which was measured by enzyme-linked immunosorbent assay (ELISA). Results: Of all treatments, rituximab wild type (WT) showed superior B cell depletion than Fc mutant rituximab. The C1q knock-out variant (rituximab-P331S) and the variant with improved affinity to Fc receptor CD16 (rituximab-GASDALIE) did not differ in depletion. A cytokine release was not detected with the treatments, however, a cytokine stimulation in NK cells was observed. Rituximab-GASDALIE had the most prominent cytokine stimulation and CD107a (marker of NK cell functional activity) expression on NK cells. Rituximab-WT and rituximab-P331S had a minor and similar cytokine stimulation and CD107a expression between each other. Rituximab-IgG2 had minimal B cell depletion, CD107a expression and cytokine stimulation. Conclusions: Rituximab depleted B cells without inducing measurable cytokine release for healthy individuals. Among the treatments, Fc mutant rituximab seem to induce less B cell depletion. Moreover, rituximab-GASDALIE appear to elicit an enhanced NK cell activation. Further studies should include more donors as supplement and the results should be interpreted as complementary data to future data analyzed by performing the loop experiment using blood from patients.
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Kravchenko, Kateryna [Verfasser]. "Development and application of standard molecules for Aβ oligomer quantification in CSF and human blood plasma in the sFIDA assay. / Kateryna Kravchenko." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2016. http://d-nb.info/1122262418/34.

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Kriel, Yusra. "The immune-modulating activity of Artemisia afra." Thesis, University of the Western Cape, 2010. http://etd.uwc.ac.za/index.php?module=etd&action=viewtitle&id=gen8Srv25Nme4_4025_1299669473.

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This study shows that herbs can be effectively screened for potiential bio-activity using in vitro methods. Further studies will be needed to better explore Artemisia afra&rsquo
s effect on immunoregulation, particularly long term effects of the herb on the immune system and its effect on other disease states.

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Rennel, Emma. "Molecular Mechanisms in Endothelial Cell Differentiation." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis : Univ.-bibl. [distributör], 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4059.

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Nguyen, Vu Khue. "Dosage de la creatinine par voie enzymatique : detection spectrophotometrique et detection electrochimique." Université Louis Pasteur (Strasbourg) (1971-2008), 1986. http://www.theses.fr/1986STR13095.

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Houng, Yu-lun, and 洪玉倫. "Comparison and improvement of assay methods for malondialdehyde levels in human blood plasma." Thesis, 1999. http://ndltd.ncl.edu.tw/handle/24140460224293046229.

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碩士
國立中興大學
食品科學系
87
ABSTRACT A common method for measurement of MDA (malondialdehyde) levels in human plasma is the TBA (thiobarbituric acid) test. Both the protocols of TBA test and the MDA levels measured as TBARS in human plasma vary widely. The specificity of the TBA reaction has been strongly questioned by various laboratories. Hence, we used the plasma of 16 volunteers to study the correlation between four commonly used methods. Furthermore, we improved the procedure of TBA test and examined the adaptability of the modified procedure. In addition, we investigated the relationship of total MDA, bound MDA and free MDA in human plasma. Th four methods used were: (1) measurement of TBARS of plasma TCA-supernatant (Method A; Radiguez-Martinez and Ruiz-Torres 1992)；(2) measurement of lipid peroxides (Method B; Yagi 1989)；(3) measurement of total MDA (Method C; Chirico et al. 1993)；(4) measurement of MDA in plasma treated with KI prior to TBA reaction (Method D; Chow and Li 1994). The results show that there were positive correlations between TBARS determined by method A and method B (r = 0.740, P<0.02) and by method C and method D (r = 0.516, P<0.05). There was a negative correlation between TBARS by method B and method D (r = 0.548, P<0.05). The results show the need of standardization of the various TBA tests. Following the TBA test protocols of each of the four methods, TBARS (or TBA-MDA adducts) were detected by spectrophotometry, flourescence and HPLC/Vis. The results show that there were significant correlations among the values obtained by the three detectors within each protocol. The TBARS obtained from the four methods with spectrophotometric detection were higher than those detected with flourescence and HPLC/Vis detection. There was a significant correlation (r = 0.889, P<0.002) between TBARS determined by method A with spectrophotometric detection and HPLC/Vis detection. Hence, method A with spectrophotometric detection could be a simple method to determine free MDA in plasma. There also was a positive correlation in lipid peroxides determined by method B between flourescence and HPLC/Vis detection (r = 0.918, P<0.001). There was no significant difference in lipid peroxides obtained from method B by flourescence detection and HPLC/Vis detection (P>0.20). Thus, most materials measured by method B should be TBA-MDA adducts rather than lipid peroxides. In order to improve the TBA test procedure, we investigated the effects of alkaline hydrolysis, types of acids, acid-heating time, BHT (butylated hydroxytoluene) and KI on levels of TBA-MDA adduct in human plasma. Results show that alkaline hydrolysis was a critical step for measurement of total MDA in plasma, because this treatment led to release of MDA from plasma proteins. TCA was a better protein precipitating reagent than H3PO4 since the TBA-MDA adduct of TCA-whole plasma did not increase after 30 min. BHT was used to inhibit the formation of lipid peroxidation during TBA test. The levels of TBA-MDA adduct were decreased 23% by inclusion of 0.2% BHT in plasma. The addition of 1% KI resulted in 43% decrease in the TBA-MDA adduct. Therefore, both BHT and KI were included in the modified procedure. The total MDA obtained from 16 volunteers by the modified procedure and detected by spectrophotometry, flourescence and HPLC/Vis were 1.92±1.04 μM, 1.81±0.92μM and 1.54±0.72μM, respectively. The differences among the three values were not significant (P>0.05). The data shows that TBARS obtained by the modified procedure were essentially TBA-MDA adduct. The recovery (average: 82~106%), precision (within-assay C.V%: 2~4%, between-assay C.V%: 4~8%) and sensitivity of the modified procedure was comparable to other methods detected by HPLC. In addition, the modified procedure with HPLC/Vis detection compared favorably with other indices of lipid peroxidation. Furthermore, we measured total MDA, bound MDA and free MDA of plasma by the modified procedure with HPLC/Vis detection. The results show that total MDA (1.45±0.17μM) was equal to bound MDA (1.34±0.07μM) plus free MDA (0.07±0.02μM). There was no significant correlation between free MDA and bound MDA (r = 0.620, n=6, P>0.05) or between free MDA and total MDA (r = 0.587, n=6, P>0.05). By contrast, bound MDA and total MDA was highly correlated (r = 0.941, n=9, P<0.001). Thus, the results indicate that the measurement of total MDA or bound MDA is a better index of lipid peroxidation than the measurement of free MDA in plasma. In conclusion, the applicability of the modified procedure is good. However, the application of the modified procedure for assessing oxidative stress in various diseases remains to be examined. Keywords Human plasma, MDA (malondialehye), lipid peroxidation, HPLC
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Books on the topic "Human blood assay"

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Reid, Christopher. The development of an automated enzyme coupled assay for glutamine detection in human blood. Sudbury, Ont: Laurentian University, 1999.

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Provan, Drew, Trevor Baglin, Inderjeet Dokal, and Johannes de Vos. Haematological investigations. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199683307.003.0016.

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Full blood count - Blood film - Plasma viscosity - ESR - Haematinic assays - Haemoglobin electrophoresis - Haptoglobin - Schumm’s test - Kleihauer test - Reticulocytes - Urinary haemosiderin - Ham’s test - Immunophenotyping - Cytogenetics - Human leucocyte antigen (HLA) typing
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Provan, Drew, Trevor Baglin, Inderjeet Dokal, Johannes de Vos, and Mammit Kaur. Haematological investigations. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199683307.003.0016_update_001.

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Full blood count - Blood film - Plasma viscosity - ESR - Haematinic assays - Haemoglobin electrophoresis - Haptoglobin - Schumm’s test - Kleihauer test - Reticulocytes - Urinary haemosiderin - Ham’s test - Immunophenotyping - Cytogenetics - Human leucocyte antigen (HLA) typing
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Fawcett, John. A study of free drug assays in human blood samples by G.L.C. 1985.

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Book chapters on the topic "Human blood assay"

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Fine, Noah, William Khoury, and Michael Glogauer. "In Vitro Assay for Sensitive Determination of Human Blood PMN Responses." In Methods in Molecular Biology, 235–41. New York, NY: Springer US, 2019. http://dx.doi.org/10.1007/978-1-0716-0154-9_18.

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Myers, Nicole T., and Stephen G. Grant. "The Blood-Based Glycophorin A (GPA) Human In Vivo Somatic Mutation Assay." In Molecular Toxicology Protocols, 223–44. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-739-6_18.

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Liebers, Verena, Benjamin Kendzia, Heike Stubel, Gerda Borowitzki, Vitali Gering, Christian Monsé, Olaf Hagemeyer, Rolf Merget, Thomas Brüning, and Monika Raulf. "Cell Activation and Cytokine Release Ex Vivo: Estimation of Reproducibility of the Whole-Blood Assay with Fresh Human Blood." In Advances in Experimental Medicine and Biology, 25–36. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/5584_2018_225.

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Schepky, Andreas, Hendrik Reuter, Jochen Kühnl, and Pierre Aeby. "Human Peripheral Blood Monocyte Derived Dendritic Cells Assay for the Detection and Characterization of Sensitizers." In Alternatives for Dermal Toxicity Testing, 331–45. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-50353-0_23.

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Hwai, Haw, Yi-Ying Chen, and Shiang-Jong Tzeng. "B-Cell ELISpot Assay to Quantify Antigen-Specific Antibody-Secreting Cells in Human Peripheral Blood Mononuclear Cells." In Methods in Molecular Biology, 133–41. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8567-8_11.

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Schattner, A., and M. Revel. "Monitoring of Interferon Therapy by Assay of Interferon-Induced (2′–5′) Oligo a Synthetase in Human Peripheral White Blood Cells." In Clinical Aspects of Interferons, 271–83. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1737-1_21.

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Sun, Peifang, and Monika Simmons. "Dendritic Cell-Based ELISpot Assay for Assessing T-Cell IFN-γ Responses in Human Peripheral Blood Mononuclear Cells to Dengue Envelope Proteins." In Methods in Molecular Biology, 187–96. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8567-8_17.

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Vocanson, Marc, Amine Achachi, Virginie Mutez, Magalie Cluzel-Tailhardat, Béatrice Le Varlet, Aurore Rozières, Philippe Fournier, and Jean-François Nicolas. "Human T Cell Priming Assay: Depletion of Peripheral Blood Lymphocytes in CD25+ Cells Improves the In Vitro Detection of Weak Allergen-Specific T Cells." In T Lymphocytes as Tools in Diagnostics and Immunotoxicology, 89–100. Basel: Springer Basel, 2013. http://dx.doi.org/10.1007/978-3-0348-0726-5_7.

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Horn, Patrick, Simone Bork, and Wolfgang Wagner. "Standardized Isolation of Human Mesenchymal Stromal Cells with Red Blood Cell Lysis." In Mesenchymal Stem Cell Assays and Applications, 23–35. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-60761-999-4_3.

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Araujo, Fernando. "Real-Time PCR Assays for High-Throughput Blood Group Genotyping." In DNA and RNA Profiling in Human Blood, 25–37. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-553-4_3.

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Conference papers on the topic "Human blood assay"

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Cunningham, Matt, Sarah Howard, Abby Beltrame, Yan Chen, and Mark Smith. "Thrombogenicity Testing for Blood-Contacting Medical Devices in an In Vitro Human Blood-Loop." In 2018 Design of Medical Devices Conference. American Society of Mechanical Engineers, 2018. http://dx.doi.org/10.1115/dmd2018-6875.

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Thrombogenicity testing continues to be a critical requirement for regulatory approval of blood-contacting medical devices and the ISO guidelines have recently been updates [1]. This new guideline ascribes value to both in vivo and in vitro testing including both the non-anticoagulated venous implant (NAVI) model, and the new methods for in vitro testing. One challenge with the animal-blood-based in vitro assays that have been validated and used for submissions is that they still may not accurately translate to clinical safety or predict the risk for thrombogenic potential in humans. We have previously described a model using minimally heparinized ovine blood and are continuing to improve the overall methodology [2,3]. In addition, we have transferred these methods to a human blood assay which therefore has enhanced potential for prediction of clinical risk. As with the ovine model, the key characteristics of a successful in vitro method include fresh blood, low levels of anticoagulation, flow conditions and minimization of air/blood interfaces. This human model integrates freshly harvested human blood containing minimal levels of heparin with variable flow from a unidirectional peristaltic pump and unlike many of the human blood assays, it can accommodate larger devices and higher flow rates than previously described [1,4]. Control materials which were optimized in the ovine model were also used to reproducibly elicit positive and negative thrombogenic responses. We feel that this model can be used for validation of the ovine model with cross comparisons of a number of legally marketed comparator devices. Alternatively, if the human blood methodology can be streamlined and performed cost effectively on a regular and basis, this assay could supplant the current ovine model and allow a highly predictive preclinical test for thrombogenicity of devices.
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Werner, Gerhard H., Dirk Boecker, Hans-Peter Haar, Hans-Juergen Kuhr, and Reinhold Mischler. "Multicomponent assay for blood substrates in human sera and haemolysed blood by mid-infrared spectroscopy." In BiOS '98 International Biomedical Optics Symposium, edited by Henry H. Mantsch and Michael Jackson. SPIE, 1998. http://dx.doi.org/10.1117/12.306074.

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Antas, P., D. Silva, A. Haushalter, and T. Sterling. "Whole Blood Assay for a Broad Assessment of Human Immune Responses toMycobacterium tuberculosisAntigens." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5911.

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Grau, E., and L. A. Moroz. "FIBRINOLYTIC ACTIVITY (FA) OF NORMAL HUMAN PERIPHERAL BLOOD MONOCYTES (MC)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644383.

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FA of blood encompasses a large cellular phase in addition to a fluid (plasma) phase. Polymorphonuclear neutrophils (PMN) have been implicated in this cellular activity, and MC have demonstrated fibrinolytic potential. Using a solid phase radiofibrin assay, we have examined FA of normal blood and plasma, and of purified PMN and MC alone, and with purified plasminogen (PLG), mini-plasminogen (mPLG) produced by gMN elastase digestion, or autologous plasma. PMN alone (0.5 x 106/mL) had striking activity (292 ± 25 SEM ng fibrin lysed/h), (n=10 normal subjects) while MC alone (0.5 x 106/ml) had mean FA of 32 ± 4 ng/h, all of which could be accounted for by contaminating PMN in the MC preparations (36 ± 8 ng/h). In comparison, mean whole blood FA wgs 72 ± 4 ng/h, and plasma FA was 22 ± 4 ng/h. When MC (0.5 x 106/ml) were assayed with PLG (2-40 yg/ml) or autologous plasma for 1 h, no significant FA was generated, indicating that neither intrinsic nor PLG-dependent (plasminogen activator, PA) activity of MC contribute significantly to the FA of whole blood as measured by routine 1 h assay, where 70% of measured FA involves the cellular phase. However, with longer assay times (2-6 h), there was time-dependent appearance of FA when MC were mixed with PLG or with autologous plasma. This FA was dependent upon interaction between MC and PLG, since no FA was generated by supernatants of MC preincubated alone, while FA was readily detected in the medium when MC and PLG were mixed. Comparing effects of PLG and mPLG, FA of MC (0.5 x 106/ml) with PLG (40 Ug/ml) was 447 ± 9 ng/3 h, while FA with mPLG (40 pg/ml, an approximate 3-fold molar excess) was 156 ± 5 ng/3 h, indicating a possible role for the N-terminal portion of the PLG molecule (containing kringle domains 1-4 absent in mPLG) in interaction ofg MC and PLG, or of MC-derived PA and PLG. FA of MC (0.5 x 106/ml) in autologous plasma (83±3 ng/3 h) was markedly reduced after lysine-Sepharose PLG depletion (14 ± 1 ng/3 h), and by addition of tranexamic acid (10 mmol/L) (5±1 ng/3 h). Thus, normal peripheral blood monocytes, like PMN, may contribute, albeit in a minor manner, to normal blood fibrinolytic activity, via PLG activation rather than direct proteolysis, and constitute an additional mechanism for interaction between cellular and fluid (plasma) phases in blood fibrinolytic activity.
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Giddings, J. C. "AN IMMUNORADIOMETRIC ASSAY (IRMA) FOR HUMANTHROMBOMODULIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643963.

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Thrombomodulin was separated from detergent-soluble fractions of human placenta using a combination of DEAE-Sepharose and thrombin-Sepharose chromatography. The final product demonstrated one major band (Mr approximately 100000) and three minor bands (Mr 40000 - 80000) on SDS-polyacrylamide gel electrophoresis. The purified protein markedly enhanced the rate of activation of human protein C by thrombin in the presence of calcium ions. Polyclonal antibodies to the isolated thrombomodulin were raised in rabbits and were shown to inhibit thrombin co-factor activity. Immunofluorescence of fibroblasts and of human umbilical vein endothelial cells in culture demonstrated that thrombomodulin antigen was specifically located in endothelial cell membranes. Affinity purified antibody was labelled with 125I and was used to establish an immunoradiometric assay (IRMA). The method was sensitive to approximately 10.0μg purified thrombomodulin per litre. The concentration of thrombomodulin in detergent-solubilised endothelial cells obtained at intervals during primary culture was proportional to the number of cells harvested for assay and appeared to reflect cell growth. Confluent cells from four experiments (approximately 2 × 106 cells per culture dish) contained on average 8.4ng thrombomodulin. Incubation of confluent endothelial cells with medium containing 1 unit per ml human α-thrombin for 10 mins at 37°C reduced the amount of cellular thrombomodulin detected in this assay by up to 30%. Assays of human plasma confirmed that low levels of thrombomodulin are present in normal circulating blood. A mean level of 160μg per litre was detected in 20 normal donors. The levels of thrombomodulin antigen in 10 normal serum were not significantly different from those in the corresponding normal plasma. Preliminary results illustrated that increased levels of thrombomodulin might be found in the plasma of some patients with a variety of clinical disorders. The data suggest that quantitative assays of thrombomodulin might provide a useful index of endothelial disturbances in vivo.
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Filippi, J. F., D. Arnoux, N. Tubiana, B. Boutière, F. Le Caär, J. Sampol, Lab Hématol, Pr J. Sampol, and Pr Y. Carcassonne. "PLASMINOGEN ACTIVATOR ACTIVITY OF NORMAL AND MALIGNANT MONONUCLEAR HUMAN CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643167.

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Plasminogen activators (PA) are thought to play a role in the invasive and metastatic properties of many types of cancer cells. Though, discrepancies in correlations between fibrinolytic activity and metastatic potential of malignant cells have been described.In this study, we evaluated both tissue type (tPA) and urokinase type (UK) cellular PA activities in different mononuclear cell types : normal T and B human peripheral lymphocytes, B cells from patients with chronic lymphocytic leukemia (CLL), human blood monocytes, alveolar macrophages, U 937, RAJI and JM cell 1ines.Mononuclear cells were isolated by Ficoll-hypaque gradients and monocytes by plastic adhesion. T and B cells were separated by a rosetting technique using sheep red blood cells. Cellular extracts were prepared by 0.5 % Triton X 100 buffer treatment followed by sonication and centrifugation 10 ' at 2000 g. PA assays were performed on the supernatants.UK-type PA was evaluated by a liquid-phase assay in presence of human plasminogen (Kabi) and chromogenic substrate S 2251 (Kabi).tPA was determinated using a solid-phase fibrin activity assay which involves an affinity separation step and thus allows selective detection of tPA.In both cases, results were reported in international units by reference to standard curves of UK (Choay) or tPA (Kabi).In all cell types tested, PA detected was essentially urokinase-type. Highest PA activity was found in U 937 cells (0.7 IU/5×l06 cells). In normal blood lymphocytes, mean PA activity was 0.08 IU/5×l06 cells. Examination of lymphocytes from patients with CLL revealed a marked decrease in UK activity as compared to normals (< 0.01 IU/5×106 cells in more than 50 % cases).The function of PA in normal lymphocyte physiology and the potential pathogenic role of diminished PA in CLL lymphocytes remains to be investigated.
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Nieschke, Kathleen, Anja Mittag, Karolina Golab, Jozsef Bocsi, Arkadiusz Pierzchalski, Wojciech Kamysz, and Attila Tarnok. "Flow cytometric assay for analysis of cytotoxic effects of potential drugs on human peripheral blood leukocytes." In SPIE BiOS, edited by Daniel L. Farkas, Dan V. Nicolau, and Robert C. Leif. SPIE, 2014. http://dx.doi.org/10.1117/12.2037741.

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8

Riethorst, W., M. W. P. M. te Booy, T. Beugeling, A. Bantjes, J. Over, and W. G. van Aken. "THE ISOLATION OF COAGULATION FACTOR VIII FROM HUMAN BLOOD PLASMA BY AFFINITY CHROMATOGRAPHY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644059.

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The need for high quality concentrates of coagulation factor VIII (FVIII:C) for treatment of haemophilia A is increasing. As the purity of FVIII:C obtained with existing large scale methods is poor and yields are low, another method for the isolation of FVIII is being developed primarily to avoid losses incurred during cryoprecipitation.Affinity gels were prepared by derivatizing Sepharose CL 4B with different positively charged ligand-spacer combinations. The adsorption of FVIII as well as the von Willebrand factor (VWF) from human blood plasma onto these gels was measured by a one-stage assay for FVIII:C, and enzyme immuno assays (ELISA) for FVIII:CAG and VWF:AG using monoclonal antibodies. The influences of pH, conductivity, ligand density, geltplasma ratio, and length and composition of the spacer as well as the adsorption kinetics were studied to obtain information about the types of interactions responsible for bonding of FVIII to the gels. A combination of at least electrostatic and hydrophobic interactions was concluded to play a role in most cases.At optimal conditions more than 90 % of FVIII could be adsorbed batch-wise from plasma at room temperature in less than one hour with a gel:plasma ratio of 1:20 (i.e. 2.5 g dried gel/1 plasma). In different runs 65-75 % of the FVIII:C applied was recovered by column-wise elution with a salt gradient. The eluate contained less than 0.34 % of the protein applied, which implies that FVIII was purified 190 times. Using fresh-frozen plasma (0.8 IU FVIII/ml) as a starting material for this one-step procedure the final specific activity was 2.3 IU/mg, which is significantly better than that obtained for FVIII isolated by cryoprecipitation. Furthermore, the F. VIII:C to VWF ratio in the eluate was approximately 1:1. The isolated FVIII:C was stable at room temperature and the supernatant plasma appears suitable for further fractionation. It is concluded that this method is worth scaling up and its use for purification of FVIII from other sources is anticipated.
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Abbink, J., J. Nuijens, C. Huijbregts, and E. Hack. "DETECTION OF INACTIVATED α2-MACROGLOBULIN (α2M) IN HUMAN PLASMA USING MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643865.

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Monoclonal antibodies (mAbs) were raised against human a2M. Five mAbs that bound to α2M in ELISA were further analyzed by a radioimmunoassay (RIA) for their reaction with three types of α2M: native α2M, chemically inactivated α2M (iα2M) (methylamine treated), and proteolytically iα2M. One mAb reacted with all forms of α2M, while four mAbs bound both forms of ia2M but not native α2M. One of these latter mAbs (Ml) was used to develop a RIA (the Ml-assay) for the detection of iα2M in plasma: Ml coupled to Sepharose is incubated with the plasma to be tested, and bound iα2M is detected by a subsequent incubation with polyclonal 125I-anti-α2M antibodies. As little as 5 ng of iα2M can be detected with this assay in the presence of an excess of native α2M. This assay was then applied to measure inactivation of α2M in vitro and in vivo. In vitro activation of the contact system in plasma by dextran sulfate results in the inactivation of ca 10% of α2M. When blood from normal donors was collected under optimal conditions, about 0.5% of the total α2M content appeared to be iα2M. Longitudinal studies in patients (a.o. with septicaemie, during cardiopulmunary bypass) revealed that increased levels of iα2M occurred sporadically. The Ml-assay appears to be useful to monitor the role of α2M in human diseases.
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Kravtsov, Alexander L., Tatyana P. Grebenyukova, Elena V. Bobyleva, Elena M. Golovko, Tatyana A. Malyukova, Mikhail N. Lyapin, Tatyana A. Kostyukova, Igor N. Yezhov, and Oleg S. Kuznetsov. "Flow cytofluorometric assay of human whole blood leukocyte DNA degradation in response to Yersinia pestis and Staphylococcus aureus." In Saratov Fall Meeting 2000, edited by Valery V. Tuchin. SPIE, 2001. http://dx.doi.org/10.1117/12.431530.

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Reports on the topic "Human blood assay"

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Nelson, Marian R., Clark L. Gross, William J. Smith, and Susan A. Kelly. Determination of ATP Levels in Sulfur Mustard-Exposed Human Peripheral Blood Lymphocytes by a Chemiluminescent Assay. Fort Belvoir, VA: Defense Technical Information Center, January 2000. http://dx.doi.org/10.21236/ada390626.

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Shpigel, Nahum, Raul Barletta, Ilan Rosenshine, and Marcelo Chaffer. Identification and characterization of Mycobacterium paratuberculosis virulence genes expressed in vivo by negative selection. United States Department of Agriculture, January 2004. http://dx.doi.org/10.32747/2004.7696510.bard.

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Mycobacterium avium subsp. paratuberculosis (MAP) is the etiological agent of a severe inflammatory bowel disease (IBD) in ruminants, known as Johne’s disease or paratuberculosis. Johne’s disease is considered to be one of the most serious diseases affecting dairy cattle both in Israel and worldwide. Heavy economic losses are incurred by dairy farmers due to the severe effect of subclinical infection on milk production, fertility, lower disease resistance and early culling. Its influence in the United States alone is staggering, causing an estimated loss of $1.5 billion to the agriculture industry every year. Isolation of MAP from intestinal tissue and blood of Crohn's patients has lead to concern that it plays a potential pathogenic role in promoting human IDB including Crohn’s disease. There is great concern following the identification of the organism in animal products and shedding of the organism to the environment by subclinically infected animals. Little is known about the molecular basis for MAP virulence. The goal of the original proposed research was to identify MAP genes that are required for the critical stage of initial infection and colonization of ruminants’ intestine by MAP. We proposed to develop and use signature tag mutagenesis (STM) screen to find MAP genes that are specifically required for survival in ruminants upon experimental infection. This research projected was approved as one-year feasibility study to prove the ability of the research team to establish the animal model for mutant screening and alternative in-vitro cell systems. In Israel, neonatal goat kids were repeatedly inoculated with either one of the following organisms; MAP K-10 strain and three transposon mutants of K-10 which were produced and screened by the US PI. Six months after the commencement of inoculation we have necropsied the goats and taken multiple tissue samples from the jejunum, ileum and mesenteric lymph nodes. Both PCR and histopathology analysis indicated on efficient MAP colonization of all the inoculated animals. We have established several systems in the Israeli PI’s laboratory; these include using IS900 PCR for the identification of MAP and using HSP65-based PCR for the differentiation between MAV and MAP. We used Southern blot analysis for the differentiation among transposon mutants of K-10. In addition the Israeli PI has set up a panel of in-vitro screening systems for MAP mutants. These include assays to test adhesion, phagocytosis and survival of MAP to/within macrophages, assays that determine the rate of MAPinduced apoptosis of macrophages and MAP-induced NO production by macrophages, and assays testing the interference with T cell ã Interferon production and T cell proliferation by MAP infected macrophages (macrophage studies were done in BoMac and RAW cell lines, mouse peritoneal macrophages and bovine peripheral blood monocytes derived macrophages, respectively). All partners involved in this project feel that we are currently on track with this novel, highly challenging and ambitious research project. We have managed to establish the above described research systems that will clearly enable us to achieve the original proposed scientific objectives. We have proven ourselves as excellent collaborative groups with very high levels of complementary expertise. The Israeli groups were very fortunate to work with the US group and in a very short time period to master numerous techniques in the field of Mycobacterium research. The Israeli group has proven its ability to run this complicated animal model. This research, if continued, may elucidate new and basic aspects related to the pathogenesis MAP. In addition the work may identify new targets for vaccine and drug development. Considering the possibility that MAP might be a cause of human Crohn’s disease, better understanding of virulence mechanisms of this organism might also be of public health interest as well.
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