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Статті в журналах з теми "Bovin hemoglobin"

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Автор: Grafiati

Опубліковано: 22 червня 2024

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1

Goldman, Daniel W., Richard J. Breyer, David Yeh, Beth A. Brockner-Ryan, and Abdu I. Alayash. "Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl iron." American Journal of Physiology-Heart and Circulatory Physiology 275, no. 3 (September 1, 1998): H1046—H1053. http://dx.doi.org/10.1152/ajpheart.1998.275.3.h1046.

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We tested the hypothesis that chemical modifications used to produce stable, oxygen-carrying, Hb-based blood substitutes can induce cytotoxicity in endothelial cells in culture because of altered redox activity. We examined the interaction of hydrogen peroxide with nonmodified hemoglobin (HbA0) and two chemically modified hemoglobins, α-cross-linked hemoglobin (α-DBBF) and its polymerized form (poly-α-DBBF). Hydrogen peroxide-induced cell death (as assessed by lactate dehydrogenase release) in bovine aortic endothelial cells (BAEC) was completely inhibited by all three hemoglobin preparations, consistent with their known pseudoperoxidase activity [hemoglobin consumes peroxide as it cycles between ferric (Fe3+) and ferryl (Fe4+) hemes]. However, reaction of the modified hemoglobins, but not HbA0, with hydrogen peroxide induced apoptotic cell death (as assessed by morphological changes and DNA fragmentation) that correlated with the formation of a long-lived ferrylhemoglobin. A preparation of ferryl-α-DBBF free of residual peroxide rapidly induced morphological changes and DNA fragmentation in BAEC, indicative of apoptotic cell death. Redox cycling of chemically modified hemoglobins by peroxide yielded a persistent ferryl iron that was cytotoxic to endothelial cells.

2

Jordan, Shane D., and Earnest Alexander. "Bovine Hemoglobin." Journal of Pharmacy Practice 26, no. 3 (August 6, 2012): 257–60. http://dx.doi.org/10.1177/0897190012451928.

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Introduction: Management of severe symptomatic anemia in critically ill Jehovah’s Witness patients remains a challenge. The paucity of therapeutic alternatives to human red blood cells has prompted the use of blood substitutes. Case Report: A 19-year-old female Jehovah’s Witness patient presented to the emergency department following several episodes of syncope. She was found to have a positive Coombs test and was diagnosed with warm-bodied autoimmune hemolytic anemia. Upon admission, her hemoglobin was 8.4 g/dL, then dropped to a nadir of 2.8 g/dL 4 days later. She received traditional management with corticosteroids, intravenous immune globulin, rituximab, and partial splenic artery embolization. Despite these therapies, hemoglobin levels failed to respond, and she experienced signs of marked ischemia. A decision was made to give 2 units of Hemopure, a bovine hemoglobin-based oxygen carrier, and the hemoglobin levels increased to 8.7 g/dL 10 days later. The patient’s overall clinical condition improved leading to subsequent hospital discharge. Conclusion: This case exemplifies the ingenuity that health care practitioners must use in critical situations involving the medical management of anemic Jehovah’s Witness patients who refuse blood products. Hemopure was used as “bridging treatment” to help save a patient from the devastating effects of ischemia resulting from severe anemia.

3

Li, Chenyang, Tao Zhang, Zhengshan Luo, Jingwen Zhou, Jianghua Li, Jian Chen, Guocheng Du, and Xinrui Zhao. "Efficient Secretory Expression for Mammalian Hemoglobins in Pichia pastoris." Fermentation 10, no. 4 (April 11, 2024): 208. http://dx.doi.org/10.3390/fermentation10040208.

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Mammalian hemoglobins (HB) are a kind of heme-binding proteins that play crucial physiological roles in various organisms. The traditional techniques employed for the extraction of HB are expensive and time-consuming, while the yields of mammalian HB in previous reports were quite low. The industrial Pichia pastoris is a highly effective platform for the secretory expression of heterologous proteins. To achieve efficient secretory expression of HB in P. pastoris, multiple strategies were applied, including the selection of a suitable host, the screening of optimal endogenous signal peptides, the knockout of VPS10, VTH1, and PEP5, and the co-expression of Alpha-Hemoglobin Stabilizing Protein (AHSP). In addition, the conditions for producing HB were optimized at shaking-flask level (BMMY medium with 100 mg/L of hemin, 2% methanol, and 24 °C). Based on these conditions, the higher titers of bovine hemoglobin (bHB, 376.9 ± 13.3 mg/L), porcine hemoglobin (pHB, 119.2 ± 7.3 mg/L), and human hemoglobin (hHB, 101.1 ± 6.7 mg/L) were achieved at fermenter level. The engineered P. pastoris strain and comprehensive strategies can also be applied to facilitate the synthesis of other high-value-added hemoproteins or hemoenzymes.

4

MATCHAM, G. W. J., J. M. CHAPSAL, and D. GUILLOCHON. "Catalytic Activities of Bovine Hemoglobin." Annals of the New York Academy of Sciences 501, no. 1 Enzyme Engine (June 1987): 21–35. http://dx.doi.org/10.1111/j.1749-6632.1987.tb45680.x.

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5

BRAEND, M., G. EFREMOV, and A. RAASTAD. "GENETICS OF BOVINE HEMOGLOBIN D." Hereditas 54, no. 3 (September 2, 2009): 255–59. http://dx.doi.org/10.1111/j.1601-5223.1966.tb02020.x.

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6

Lima, Maria Celiana P., and Cristina T. Andrade. "Stroma-Free Hemoglobin from Bovine Blood." Artificial Cells, Blood Substitutes, and Biotechnology 35, no. 4 (January 2007): 431–47. http://dx.doi.org/10.1080/10731190701460333.

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7

Shirahama, Hiroyuki, Koji Suzuki, and Toshiro Suzawa. "Bovine hemoglobin adsorption onto polymer latices." Journal of Colloid and Interface Science 129, no. 2 (May 1989): 483–90. http://dx.doi.org/10.1016/0021-9797(89)90462-1.

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8

Clementi, Maria E., Roberto Scatena, Alvaro Mordente, Saverio G. Condò, Massimo Castagnola, and Bruno Giardina. "Oxygen Transport by Fetal Bovine Hemoglobin." Journal of Molecular Biology 255, no. 1 (January 1996): 229–34. http://dx.doi.org/10.1006/jmbi.1996.0019.

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9

Salzano, A. M., A. Pauciullo, D. Ambrosio C, G. Novi, M. Strazzullo, and A. Scaloni. "Bovine hemoglobin polymorphism: a novel alpha-globin variant identified in the Agerolese breed from southern Italy." Czech Journal of Animal Science 60, No. 4 (July 15, 2016): 145–51. http://dx.doi.org/10.17221/8128-cjas.

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10

Wang, Ying, Linli Wang, Weili Yu, Dawei Gao, Guoxing You, Penglong Li, Shan Zhang, et al. "A PEGylated bovine hemoglobin as a potent hemoglobin-based oxygen carrier." Biotechnology Progress 33, no. 1 (October 31, 2016): 252–60. http://dx.doi.org/10.1002/btpr.2380.

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11

D'Agnillo, Felice. "Redox active hemoglobin enhances lipopolysaccharide-induced injury to cultured bovine endothelial cells." American Journal of Physiology-Heart and Circulatory Physiology 287, no. 4 (October 2004): H1875—H1882. http://dx.doi.org/10.1152/ajpheart.00164.2004.

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The interaction of cell-free hemoglobin with lipopolysaccharide (LPS) is thought to aggravate the pathophysiology of sepsis and/or septic shock. This study examines the possible modulatory role of cell-free hemoglobin on LPS-induced apoptosis of cultured bovine aortic endothelial cells. Experiments were performed with or without fetal bovine serum, a source of LPS-binding protein and soluble CD14. In the absence of serum, LPS alone or coincubated with purified bovine hemoglobin (BvHb), human hemoglobin (Hb), or α-cross-linked Hb (ααHb) did not induce apoptosis. In the presence of serum, LPS induced significant apoptosis. LPS combined with BvHb, Hb, or ααHb produced the same extent of apoptosis as LPS alone. To examine whether the H2O2-driven redox activity of hemoglobin alters LPS-induced apoptosis, glucose oxidase was added to the system to generate a subtoxic flux of H2O2. The combined treatment of LPS, glucose oxidase, and BvHb, Hb, or ααHb enhanced apoptosis compared with LPS alone. These findings support a possible mechanism whereby the redox cycling of hemoglobin, and not its direct interaction with LPS, contributes to the hemoglobin-mediated enhancement of LPS-related pathophysiology.

12

Condò, Saverio G., Said El-Sherbini, and Bruno Giardina. "Temperature modulation of bovine hemoglobins." Biochemical and Biophysical Research Communications 177, no. 3 (June 1991): 956–62. http://dx.doi.org/10.1016/0006-291x(91)90631-g.

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13

Lasne, Françoise, Nathalie Crepin, Michael Ashenden, Michel Audran, and Jacques de Ceaurriz. "Detection of Hemoglobin-Based Oxygen Carriers in Human Serum for Doping Analysis: Screening by Electrophoresis." Clinical Chemistry 50, no. 2 (February 1, 2004): 410–15. http://dx.doi.org/10.1373/clinchem.2003.026583.

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Abstract Background: Hemoglobin-based oxygen carriers (HBOCs) have recently been included in the International Olympic Committee and World Anti-Doping Agency lists of substances and methods prohibited in sports. To enforce this rule and deter abuse of HBOCs in elite sports, it is necessary to develop HBOC-specific screening and confirmation tests that are the usual steps in antidoping control analysis. Methods: We developed a screening method based on electrophoresis of serum samples cleared of haptoglobin (Hp). Four successive steps (immunoprecipitation of Hp, electrophoresis of the cleared serum, Western blotting of the separated proteins, and detection of hemoglobin-related molecules based on the peroxidase properties of the heme moiety), provided electropherograms that could be easily interpreted in terms of the presence of HBOCs. This method was tested with serum samples enriched with various types of HBOCs: polymerized, conjugated, and cross-linked hemoglobins. It was also applied to blood samples collected from 12 healthy volunteers who had been infused with either 30 or 45 g of Hemopure, a glutaraldehyde-polymerized bovine hemoglobin. Results: The method clearly detected the presence in serum of the various types of HBOCs tested and demonstrated no possible confusion with endogenous hemoglobin that may be present in cases of hemolysis. The test was able to detect Hemopure for 4–5 days after administration of 45 g to healthy individuals. Conclusions: The electrophoretic method is a simple, fast, and sensitive procedure that appears to fulfill the criteria of a screening test for the presence of HBOCs in antidoping control samples.

14

Dang, Meng, Qiliang Deng, Guozhen Fang, Dongdong Zhang, Jingmin Liu, and Shuo Wang. "Preparation of novel anionic polymeric ionic liquid materials and their potential application to protein adsorption." Journal of Materials Chemistry B 5, no. 31 (2017): 6339–47. http://dx.doi.org/10.1039/c7tb01234a.

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15

Marta, Maurizio, Maria Patamia, Alessandro Lupi, Mirca Antenucci, Mario Di Iorio, Sergio Romeo, Raffaele Petruzzelli, Massimo Pomponi, and Bruno Giardina. "Bovine Hemoglobin Cross-Linked through the Chains." Journal of Biological Chemistry 271, no. 13 (March 29, 1996): 7473–78. http://dx.doi.org/10.1074/jbc.271.13.7473.

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16

Cempel, Nathalie, Didier Guillochon, and Jean-Marie Piot. "Preparation of Photodynamic Hydrolyzates from Bovine Hemoglobin." Journal of Agricultural and Food Chemistry 42, no. 9 (September 1994): 2059–63. http://dx.doi.org/10.1021/jf00045a042.

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17

Maghraby, Ahmed Mohamed, and Maha Anwar Ali. "Spectroscopic study of gamma irradiated bovine hemoglobin." Radiation Physics and Chemistry 76, no. 10 (October 2007): 1600–1605. http://dx.doi.org/10.1016/j.radphyschem.2007.01.008.

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18

Daoud, Rachid, Veronique Dubois, Loredana Bors-Dodita, Naima Nedjar-Arroume, Francois Krier, Nour-Eddine Chihib, Patrice Mary, Mostafa Kouach, Gilbert Briand, and Didier Guillochon. "New antibacterial peptide derived from bovine hemoglobin." Peptides 26, no. 5 (May 2005): 713–19. http://dx.doi.org/10.1016/j.peptides.2004.12.008.

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19

Trujillo, Edward M. "Osmotic pressure measurements of dissociating bovine hemoglobin." Journal of Membrane Science 69, no. 3 (May 1992): 213–22. http://dx.doi.org/10.1016/0376-7388(92)80040-q.

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20

Outman, Ahlam, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Bernard Gressier, Bruno Eto та Naïma Nedjar. "Potential of Human Hemoglobin as a Source of Bioactive Peptides: Comparative Study of Enzymatic Hydrolysis with Bovine Hemoglobin and the Production of Active Peptide α137–141". International Journal of Molecular Sciences 24, № 15 (25 липня 2023): 11921. http://dx.doi.org/10.3390/ijms241511921.

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Cruor, the main component responsible for the red color of mammalian blood, contains 90% haemoglobin, a protein considered to be a rich source of bioactive peptides. The aim of the present study is to assess the potential of human hemoglobin as a source of bioactive peptides, compared with bovine hemoglobin, which has been extensively studied in recent years. More specifically, the study focused on the α137–141 fragment of bovine haemoglobin (TSKYR), a small (653 Da) hydrophilic antimicrobial peptide. In this work, the potential of human hemoglobin to contain bioactive peptides was first investigated in silico in comparison with bovine hemoglobin-derived peptides using bioinformatics tools. The blast results showed a high identity, 88% and 85% respectively, indicating a high similarity between the α and β chains. Peptide Cutter software was used to predict cleavage sites during peptide hydrolysis, revealing major conservation in the number and location of cleavage sites between the two species, while highlighting some differences. Some peptides were conserved, notably our target peptide (TSKYR), while others were specific to each species. Secondly, the two types of hemoglobin were subjected to similar enzymatic hydrolysis conditions (23 °C, pH 3.5), which showed that the hydrolysis of human hemoglobin followed the same reaction mechanism as the hydrolysis of bovine hemoglobin, the ‘zipper’ mechanism. Concerning the peptide of interest, α137–141, the RP-UPLC analyses showed that its identification was not affected by the increase in the initial substrate concentration. Its production was rapid, with more than 60% of the total α137–141 peptide production achieved in just 30 min of hydrolysis, reaching peak production at 3 h. Furthermore, increasing the substrate concentration from 1% to 10% (w/v) resulted in a proportional increase in α137–141 production, with a maximum concentration reaching 687.98 ± 75.77 mg·L−1, approximately ten-fold higher than that obtained with a 1% (w/v) concentration. Finally, the results of the UPLC-MS/MS analysis revealed the identification of 217 unique peptides in bovine hemoglobin hydrolysate and 189 unique peptides in human hemoglobin hydrolysate. Of these, 57 peptides were strictly common to both species. This revealed the presence of several bioactive peptides in both cattle and humans. Although some had been known previously, new bioactive peptides were discovered in human hemoglobin, such as four antibacterial peptides (α37–46 PTTKTYFPHF, α36–45 FPTTKTYFPH, α137–141 TSKYR, and α133–141 STVLTSKYR), three opioid peptides (α137–141 TSKYR,β31–40 LVVYPWTQRF,β32–40, VVYPWTQRF), an ACE inhibitor (β129–135 KVVAGVA), an anticancer agent (β33–39 VVYPWTQ), and an antioxidant (α137–141 TSKYR). To the best of our knowledge, these peptides have never been found in human hemoglobin before.

21

Marva, E., and RP Hebbel. "Denaturing interaction between sickle hemoglobin and phosphatidylserine liposomes." Blood 83, no. 1 (January 1, 1994): 242–49. http://dx.doi.org/10.1182/blood.v83.1.242.242.

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Abstract It is hypothesized that abnormal interaction between sickle hemoglobin (HbS) and erythrocyte membrane lipid might promote deposition of denatured hemoglobin (hemichrome) on the membrane. We compared the interaction of HbS and normal HbA with large unilamellar phosphatidylserine (PS) liposomes under low salt/pH conditions. Admixture of oxyHb and dioleoyl-PS resulted in loss of absorbance at 412 nm, the apparent first order rate constant for which was .25 +/- 0.02 hour-1 for HbA and .85 +/- 0.18 hour-1 for HbS. This was ascribable largely to formation of metHb and hemichromes and was accompanied by some actual transfer of heme from hemoglobin to lipid phase. By comparison, admixture of oxyHb with liposomes made from bovine brain PS having unsaturated acyl chains promoted even faster absorbance loss if the starting liposomal material contained detectable peroxidation by-product. In such cases, actual heme destruction developed with accompanying liberation of free iron and promotion of lipidperoxidation. Fluorescence quenching experiments indicate that hemoglobin/lipid interaction is characterized by very rapid initial electrostatic interaction, followed by development of irreversible changes. Similar changes still occur under conditions of physiologic salt/pH, but they develop much more slowly. The 3.4-fold faster oxidation of HbS versus HbA on lipid observed here represents an additional augmentation of the disparity in oxidation rates for hemoglobins in solution (1.7-fold faster for HbS than for HbA) observed previously. The accelerated promotion of Hb denaturation resulting from lipid contact may help explain deposits of hemichrome on sickle red blood cell membranes, particularly because these cells are in double jeopardy by virtue of having both the mutant HbS and abnormal amounts of peroxidized membrane lipid.

22

Marva, E., and RP Hebbel. "Denaturing interaction between sickle hemoglobin and phosphatidylserine liposomes." Blood 83, no. 1 (January 1, 1994): 242–49. http://dx.doi.org/10.1182/blood.v83.1.242.bloodjournal831242.

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It is hypothesized that abnormal interaction between sickle hemoglobin (HbS) and erythrocyte membrane lipid might promote deposition of denatured hemoglobin (hemichrome) on the membrane. We compared the interaction of HbS and normal HbA with large unilamellar phosphatidylserine (PS) liposomes under low salt/pH conditions. Admixture of oxyHb and dioleoyl-PS resulted in loss of absorbance at 412 nm, the apparent first order rate constant for which was .25 +/- 0.02 hour-1 for HbA and .85 +/- 0.18 hour-1 for HbS. This was ascribable largely to formation of metHb and hemichromes and was accompanied by some actual transfer of heme from hemoglobin to lipid phase. By comparison, admixture of oxyHb with liposomes made from bovine brain PS having unsaturated acyl chains promoted even faster absorbance loss if the starting liposomal material contained detectable peroxidation by-product. In such cases, actual heme destruction developed with accompanying liberation of free iron and promotion of lipidperoxidation. Fluorescence quenching experiments indicate that hemoglobin/lipid interaction is characterized by very rapid initial electrostatic interaction, followed by development of irreversible changes. Similar changes still occur under conditions of physiologic salt/pH, but they develop much more slowly. The 3.4-fold faster oxidation of HbS versus HbA on lipid observed here represents an additional augmentation of the disparity in oxidation rates for hemoglobins in solution (1.7-fold faster for HbS than for HbA) observed previously. The accelerated promotion of Hb denaturation resulting from lipid contact may help explain deposits of hemichrome on sickle red blood cell membranes, particularly because these cells are in double jeopardy by virtue of having both the mutant HbS and abnormal amounts of peroxidized membrane lipid.

23

Maas, Bart H. A., Anneke Buursma, Rob A. J. Ernst, Anton H. J. Maas, and Willem G. Zijlstra. "Lyophilized bovine hemoglobin as a possible reference material for the determination of hemoglobin derivatives in human blood." Clinical Chemistry 44, no. 11 (November 1, 1998): 2331–39. http://dx.doi.org/10.1093/clinchem/44.11.2331.

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Abstract We investigated the suitability of a lyophilized bovine hemoglobin (LBH) preparation containing various fractions of oxyhemoglobin (O2Hb), carboxyhemoglobin (COHb), and methemoglobin (MetHb) for quality assessment in multicomponent analysis (MCA) of hemoglobin derivatives. It was demonstrated that a stable preparation of these components after reconstitution yields a hemoglobin solution that is spectrophotometrically equivalent with a fresh bovine hemoglobin solution. The preparation was found to be stable for at least 1 year when it is kept at 2–8 °C and for 1 h after reconstitution. We determined the fractions of O2Hb, COHb, and MetHb of several LBH preparations, using the complete spectra of 480–650 nm with 2-nm intervals and absorptivities as determined for pure LBH solutions. A field trial involving various types of multiwavelength hemoglobin photometers showed the suitability of LBH as a quality-control material. Computer models of the various common multiwavelength hemoglobin photometers may be useful for establishing more accurate target values of LBH preparations for each type of photometer and for studying the importance of the influence of specific factors such as wavelength selection, absorptivity values, and interfering dyes.

24

Outman, Ahlam, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Jihen Dhaouefi, Bernard Gressier, Bruno Eto та Naïma Nedjar. "Comparison of the Bioactive Properties of Human and Bovine Hemoglobin Hydrolysates Obtained by Enzymatic Hydrolysis: Antimicrobial and Antioxidant Potential of the Active Peptide α137-141". International Journal of Molecular Sciences 24, № 17 (22 серпня 2023): 13055. http://dx.doi.org/10.3390/ijms241713055.

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This study focuses on the enzymatic hydrolysis of hemoglobin, the main component of cruor that gives blood its red color in mammals. The antibacterial and antioxidant potentials of human hemoglobin hydrolysates were evaluated in comparison to bovine hemoglobin. The results showed strong antimicrobial activity of the peptide hydrolysates against six bacterial strains, independent of the initial substrate concentration level. The hydrolysates also showed strong antioxidant activity, as measured by four different tests. In addition, the antimicrobial and antioxidant activities of the human and bovine hemoglobin hydrolysates showed little or no significant difference, with only the concentration level being the determining factor in their activity. The results of the mass spectrometry study showed the presence of a number of bioactive peptides, the majority of which have characteristics similar to those mentioned in the literature. New bioactive peptides were also identified in human hemoglobin, such as the antibacterial peptides PTTKTYFPHF (α37-46), FPTTKTYFPH (α36-45), TSKYR (α137-141), and STVLTSKYR (α133-141), as well as the antioxidant TSKYR (α137-141). According to these findings, human hemoglobin represents a promising source of bioactive peptides beneficial to the food or pharmaceutical industries.

25

Asmari, Abdulrahman K. Al. "Gastric antisecretory and antiulcer activity of bovine hemoglobin." World Journal of Gastroenterology 19, no. 21 (2013): 3291. http://dx.doi.org/10.3748/wjg.v19.i21.3291.

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26

Hu, Tao, Dongxia Li, and Zhiguo Su. "Preparation and Characterization of Dimeric Bovine Hemoglobin Tetramers." Journal of Protein Chemistry 22, no. 5 (July 2003): 411–16. http://dx.doi.org/10.1023/b:jopc.0000005455.94103.b8.

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27

Nedjar-Arroume, Naïma, Véronique Dubois-Delval, Estelle Yaba Adje, Jonathan Traisnel, François Krier, Patrice Mary, Mostafa Kouach, Gilbert Briand, and Didier Guillochon. "Bovine hemoglobin: An attractive source of antibacterial peptides." Peptides 29, no. 6 (June 2008): 969–77. http://dx.doi.org/10.1016/j.peptides.2008.01.011.

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28

Zhang, Hong-Mei, Yan-Qing Wang, Qiu-Hua Zhou, and Guang-Li Wang. "Molecular interaction between phosphomolybdate acid and bovine hemoglobin." Journal of Molecular Structure 921, no. 1-3 (March 2009): 156–62. http://dx.doi.org/10.1016/j.molstruc.2008.12.049.

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29

Gotshall, Robert W., Karyn L. Hamilton, Benjamin Foreman, Martha C. Tissot van Patot, and David C. Irwin. "Glutaraldehyde-polymerized bovine hemoglobin and phosphodiesterase-5 inhibition*." Critical Care Medicine 37, no. 6 (June 2009): 1988–93. http://dx.doi.org/10.1097/ccm.0b013e3181a00597.

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30

Ge, Moyan, Yi Shen, Weiming Chen, Yaotian Peng, and Ziyan Pan. "Adsorption of Bovine Hemoglobin by Sulfonated Polystyrene Nanospheres." ChemistrySelect 4, no. 10 (March 8, 2019): 2874–80. http://dx.doi.org/10.1002/slct.201803780.

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31

Chi, Zhenxing, Rutao Liu, Bingjun Yang, and Hao Zhang. "Toxic interaction mechanism between oxytetracycline and bovine hemoglobin." Journal of Hazardous Materials 180, no. 1-3 (August 15, 2010): 741–47. http://dx.doi.org/10.1016/j.jhazmat.2010.04.110.

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32

Soma, Lawrence R., Cornelius E. Uboh, Fuyu Guan, Yi Luo, Peter J. Moate, Raymond C. Boston, and Bernd Driessen. "The Pharmacokinetics of Hemoglobin-Based Oxygen Carrier Hemoglobin Glutamer-200 Bovine in the Horse." Anesthesia & Analgesia 100, no. 6 (June 2005): 1570–75. http://dx.doi.org/10.1213/01.ane.0000154081.38466.09.

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33

Soma, LR, F. Guan, CE Uboh, Y. Luo, PJ Moate, and B. Driessen. "Pharmacokinetics of hemoglobin-based oxygen carrier hemoglobin-glutamer-200 bovine (oxyglobin) in the horse." Veterinary Anaesthesia and Analgesia 32, no. 4 (July 2005): 17. http://dx.doi.org/10.1111/j.1467-2995.2005.00232a_35.x.

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34

Gasthuys, Maryline, Sandra Alves, and Jean-Claude Tabet. "N-Terminal Adducts of Bovine Hemoglobin with Glutaraldehyde in a Hemoglobin-Based Oxygen Carrier." Analytical Chemistry 77, no. 10 (May 2005): 3372–78. http://dx.doi.org/10.1021/ac048107i.

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Lurie, Fedor, Jonathan S. Jahr, and Bernd Driessen. "The Novel HemoCue® Plasma/Low Hemoglobin System Accurately Measures Small Concentrations of Three Different Hemoglobin-Based Oxygen Carriers in Plasma: Hemoglobin Glutamer-200 (Bovine) (Oxyglobin®), Hemoglobin Glutamer-250 (Bovine) (Hemopure®), and Hemoglobin-Raffimer (Hemolink™)." Anesthesia & Analgesia 95, no. 4 (October 2002): 870–73. http://dx.doi.org/10.1213/00000539-200210000-00014.

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36

Lurie, Fedor, Jonathan S. Jahr, and Bernd Driessen. "The Novel HemoCue® Plasma/Low Hemoglobin System Accurately Measures Small Concentrations of Three Different Hemoglobin-Based Oxygen Carriers in Plasma: Hemoglobin Glutamer-200 (Bovine) (Oxyglobin®), Hemoglobin Glutamer-250 (Bovine) (Hemopure®), and Hemoglobin-Raffimer (Hemolink™)." Anesthesia & Analgesia 95, no. 4 (October 2002): 870–73. http://dx.doi.org/10.1097/00000539-200210000-00014.

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37

Nogueira, Nadir N., Célia Colli, and Silvia M. F. Cozzolino. "Controle da anemia ferropriva em pré-escolares por meio da fortificação de alimento com concentrado de Hemoglobina Bovina (estudo preliminar)." Cadernos de Saúde Pública 8, no. 4 (December 1992): 459–65. http://dx.doi.org/10.1590/s0102-311x1992000400011.

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O efeito da introdução de biscoitos fortificados com ferro hemínico no estado de nutrição de ferro de pré-escolares foi avaliado em um estudo piloto que inclui 16 crianças, com idade entre 2 e 4 anos, de uma creche pública do estado do Piauí. A fonte de ferro utilizada foi o sangue bovino seco pelo processo de leito de jorro, uma alternativa para a secagem em spray, adaptada para a secagem de sangue. À primeira tomada de amostra, detectou-se anemia (Hb < 11 g/dL) em 12 crianças (75%). O valor médio de Hb foi de 9,4 2,6 g/dL. Os biscoitos fortificados com 3% de concentrado de hemoglobina bovina foram introduzidos na dieta oferecida (5 biscoitos (4mg Fe)/d) durante 3 meses. Após esse período, houve aumento da concentração de hemoglobina em todas as crianças e ausência de anemia (Hb = 13,2 0,2 g/dL). Os resultados obtidos apontam para a utilização do sangue total seco como uma fonte de ferro hemínico possível de ser utilizada na fortificação de alimentos, principalmente dirigidos a grupos de risco de anemia por deficiência de ferro, como é o caso dos pré-escolares.

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Abou-Diab, Mira, Jacinthe Thibodeau, Ismail Fliss, Pascal Dhulster, Laurent Bazinet, and Naima Nedjar. "Production of Demineralized Antibacterial, Antifungal and Antioxidant Peptides from Bovine Hemoglobin Using an Optimized Multiple-Step System: Electrodialysis with Bipolar Membrane." Membranes 12, no. 5 (May 11, 2022): 512. http://dx.doi.org/10.3390/membranes12050512.

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Numerous studies have shown that bovine hemoglobin, a protein from slaughterhouse waste, has important biological potential after conventional enzymatic hydrolysis. However, the active peptides could not be considered pure since they contained mineral salts. Therefore, an optimized multi-step process of electrodialysis with bipolar membranes (EDBM) was carried out to produce discolored and demineralized peptides without the addition of chemical agents. The aim of this study was to test the antibacterial, antifungal and antioxidant activities of discolored and demineralized bovine hemoglobin hydrolysates recovered by EDBM and to compare them with raw and discolored hydrolysates derived from conventional hydrolysis. The results demonstrate that discolored–demineralized hydrolysates recovered from EDBM had significant antimicrobial activity against many bacterial (gram-positive and gram-negative) and fungal (molds and yeast) strains. Concerning antibacterial activity, lower MIC values for hydrolysates were registered against Staphylococcus aureus, Kocuria rhizophila and Listeria monocytogenes. For antifungal activity, lower MIC values for hydrolysates were registered against Paecilomyces spp., Rhodotorula mucilaginosa and Mucor racemosus. Hemoglobin hydrolysates showed fungicidal mechanisms towards these fungal strains since the MFC/MIC ratio was ≤4. The hydrolysates also showed a potent antioxidant effect in four different antioxidant tests. Consequently, they can be considered promising natural, low-salt food preservatives. To the best of our knowledge, no previous studies have identified the biological properties of discolored and demineralized bovine hemoglobin hydrolysates.

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Maity, Mritunjoy, Sandip Dolui, and Nakul C. Maiti. "Hydrogen bonding plays a significant role in the binding of coomassie brilliant blue-R to hemoglobin: FT-IR, fluorescence and molecular dynamics studies." Physical Chemistry Chemical Physics 17, no. 46 (2015): 31216–27. http://dx.doi.org/10.1039/c5cp04661k.

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Williams, Alexander T., Alfredo Lucas, Cynthia R. Muller, Crystal Bolden-Rush, Andre F. Palmer, and Pedro Cabrales. "Balance between oxygen transport and blood rheology during resuscitation from hemorrhagic shock with polymerized bovine hemoglobin." Journal of Applied Physiology 129, no. 1 (July 1, 2020): 97–107. http://dx.doi.org/10.1152/japplphysiol.00016.2020.

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Large-molecular diameter polymerized bovine hemoglobin avoided vasoconstriction and impairment of cardiac function during resuscitation from hemorrhagic shock that was seen with previous hemoglobin-based O2 carriers by increasing blood viscosity in a concentration-dependent manner. Supplementation of O2-carrying capacity played a smaller role in maintaining cardiac function than increased blood and plasma viscosity.

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Outman, Ahlam, Mohamed Bouhrim, Codjo Hountondji, Omar M. Noman, Ali S. Alqahtani, Bernard Gressier, Naïma Nedjar, and Bruno Eto. "Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin." International Journal of Molecular Sciences 24, no. 20 (October 19, 2023): 15383. http://dx.doi.org/10.3390/ijms242015383.

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Enzymatic hydrolysis of bovine and human hemoglobin generates a diversity of bioactive peptides, mainly recognized for their antimicrobial properties. However, antimicrobial peptides stand out for their ability to specifically target cancer cells while preserving rapidly proliferating healthy cells. This study focuses on the production of bioactive peptides from hemoglobin and evaluates their anticancer potential using two distinct approaches. The first approach is based on the use of a rapid screening method aimed at blocking host cell protein synthesis to evaluate candidate anticancer peptides, using Lepidium sativum seed germination as an indicator. The results show that: (1) The degree of hydrolysis (DH) significantly influences the production of bioactive peptides. DH levels of 3 to 10% produce a considerably stronger inhibition of radicle growth than DH 0 (the native form of hemoglobin), with an intensity three to four times greater. (2) Certain peptide fractions of bovine hemoglobin have a higher activity than those of human hemoglobin. (3) The structural characteristics of peptides (random coil or alpha helix) play a crucial role in the biological effects observed. (4) The α137–141 peptide, the target of the study, was the most active of the fractions obtained from bovine hemoglobin (IC50 = 29 ± 1 µg/mL) and human hemoglobin (IC50 = 48 ± 2 µg/mL), proving to be 10 to 15 times more potent than the other hemoglobin fractions, attributed to its strong antimicrobial potential. The second approach to assessing anticancer activity is based on the preliminary in vitro analysis of hydrolysates and their peptide fractions, with a focus on the eL42 protein. This protein is of major interest due to its overexpression in all cancer cells, making it an attractive potential target for the development of anticancer molecules. With this in mind, astudy was undertaken using a method for labeling formylase (formyl-methionyl-tRNA transformylase (FMTS)) with oxidized tRNA. This approach was chosen because of the similarities in the interaction between formylase and the eL42 protein with oxidized tRNA. The results obtained not only confirmed the previous conclusions but also reinforced the hypothesis that the inhibition of protein synthesis plays a key role in the anticancer mechanism of these peptides. Indeed, the data suggest that samples containing α137–141 peptide (NKT) and total hydrolysates may have modulatory effects on the interaction between FMTS and oxidized tRNA. This observation highlights the possibility that the latter could influence molecular binding mechanisms, potentially resulting in a competitive situation where the ability of substrate tRNA to bind efficiently to ribosomal protein is compromised in their presence. Ultimately, these results suggest the feasibility of obtaining candidate peptides for biological anticancer drugs from both human and bovine hemoglobin sources. These scientific advances show new hope in the fight against cancer, which affects a large number of people around the world.

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Das, Sourav, Nikita Bora, Mostofa Ataur Rohman, Raju Sharma, Anupam Nath Jha, and Atanu Singha Roy. "Molecular recognition of bio-active flavonoids quercetin and rutin by bovine hemoglobin: an overview of the binding mechanism, thermodynamics and structural aspects through multi-spectroscopic and molecular dynamics simulation studies." Physical Chemistry Chemical Physics 20, no. 33 (2018): 21668–84. http://dx.doi.org/10.1039/c8cp02760a.

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Sheffield, CL, and JR DeLoach. "Preparation and in vivo evaluation of two bovine hemoglobin‐based plasma expanders." Biotechnology and Applied Biochemistry 12, no. 6 (December 1990): 630–42. http://dx.doi.org/10.1111/j.1470-8744.1990.tb00137.x.

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A hemoglobin (Hb)‐based oxygen carrier was successfully transfused into rats. An ultrapure lipid‐free bovine Hb was prepared by hypotonic dialysis and ultrafiltration. The Hb was polymerized with glutaraldehyde and the P50 was 24.3 mm Hg. On the basis of immunological analysis, immuno‐dot blot, the Hb preparations were not antigenic. A second transfusion produced no adverse immunological side effects. A right shift in P50 was obtained by further treatment of polymerized Hb with inositol hexaphosphate; however, this Hb preparation was unsuitable for transfusion as all animals died within a few minutes. A 30% exchange transfusion in rats with the polymerized bovine Hb resulted in a 100% survival of all animals. P50 values of treated animals were reduced by about 2 mm Hg for 14 days. The Hb product circulated for 14 days as determined by 51Cr labeling. Ultrapure bovine Hb has the potential to circulate and carry oxygen in rats and causes no immunological side effects.

44

Zhang, Zhifeng, Wenwen Wang, Zhentan Lu, Ke Liu, Qiongzhen Liu, and Dong Wang. "Facile fabrication of poly(glycidyl methacrylate)-b-polystyrene functional fibers under a shear field and immobilization of hemoglobin." New Journal of Chemistry 42, no. 11 (2018): 8537–43. http://dx.doi.org/10.1039/c8nj00198g.

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45

Bu, Fengrong, Heyao Wang, and Xiaoxia Zhu. "Studies on the Resuscitative Efficacy of Polymerized Bovine Hemoglobin." Artificial Cells, Blood Substitutes, and Biotechnology 28, no. 6 (2000): 493–501. http://dx.doi.org/10.3109/10731190009139266.

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46

Bucci, Enrico, Clara Fronticelli, Charles Orth, Maria Cristina Martorana, Luisa Aebischer, and Pasquale Angeloni. "Bovine Hemoglobin as a Basis for Artificial Oxygen Carriers." Biomaterials, Artificial Cells and Artificial Organs 16, no. 1-3 (January 1988): 197–204. http://dx.doi.org/10.3109/10731198809132569.

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Bradley, R., S. Sloshberg, K. Nho, B. Czuba, D. Szesko, and R. Shorr. "Production of Peg-Modified Bovine Hemoglobin: Economics and Feasibility." Artificial Cells, Blood Substitutes, and Biotechnology 22, no. 3 (January 1994): 657–67. http://dx.doi.org/10.3109/10731199409117896.

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Ouellet, H., Y. Ouellet, C. Richard, M. Labarre, B. Wittenberg, J. Wittenberg, and M. Guertin. "Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide." Proceedings of the National Academy of Sciences 99, no. 9 (April 16, 2002): 5902–7. http://dx.doi.org/10.1073/pnas.092017799.

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49

Li, Sha, Hongyuan Shang, Fasheng Liu, Min Ma, and Aiping Zhang. "Toxic effects of copper (II) ions on bovine hemoglobin." Spectroscopy Letters 51, no. 2 (February 7, 2018): 67–73. http://dx.doi.org/10.1080/00387010.2017.1335754.

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50

Bu, Fengrong, Heyao Wang, and Xiaoxia Zhu. "Studies on the Resuscitative Efficacy of Polymerized Bovine Hemoglobin." Artificial Cells, Blood Substitutes, and Biotechnology 28, no. 6 (January 2000): 493–501. http://dx.doi.org/10.1080/10731190009139266.

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