Zeitschriftenartikel zum Thema „Bovin hemoglobin“
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Goldman, Daniel W., Richard J. Breyer, David Yeh, Beth A. Brockner-Ryan und Abdu I. Alayash. „Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl iron“. American Journal of Physiology-Heart and Circulatory Physiology 275, Nr. 3 (01.09.1998): H1046—H1053. http://dx.doi.org/10.1152/ajpheart.1998.275.3.h1046.
Jordan, Shane D., und Earnest Alexander. „Bovine Hemoglobin“. Journal of Pharmacy Practice 26, Nr. 3 (06.08.2012): 257–60. http://dx.doi.org/10.1177/0897190012451928.
Li, Chenyang, Tao Zhang, Zhengshan Luo, Jingwen Zhou, Jianghua Li, Jian Chen, Guocheng Du und Xinrui Zhao. „Efficient Secretory Expression for Mammalian Hemoglobins in Pichia pastoris“. Fermentation 10, Nr. 4 (11.04.2024): 208. http://dx.doi.org/10.3390/fermentation10040208.
MATCHAM, G. W. J., J. M. CHAPSAL und D. GUILLOCHON. „Catalytic Activities of Bovine Hemoglobin“. Annals of the New York Academy of Sciences 501, Nr. 1 Enzyme Engine (Juni 1987): 21–35. http://dx.doi.org/10.1111/j.1749-6632.1987.tb45680.x.
BRAEND, M., G. EFREMOV und A. RAASTAD. „GENETICS OF BOVINE HEMOGLOBIN D“. Hereditas 54, Nr. 3 (02.09.2009): 255–59. http://dx.doi.org/10.1111/j.1601-5223.1966.tb02020.x.
Lima, Maria Celiana P., und Cristina T. Andrade. „Stroma-Free Hemoglobin from Bovine Blood“. Artificial Cells, Blood Substitutes, and Biotechnology 35, Nr. 4 (Januar 2007): 431–47. http://dx.doi.org/10.1080/10731190701460333.
Shirahama, Hiroyuki, Koji Suzuki und Toshiro Suzawa. „Bovine hemoglobin adsorption onto polymer latices“. Journal of Colloid and Interface Science 129, Nr. 2 (Mai 1989): 483–90. http://dx.doi.org/10.1016/0021-9797(89)90462-1.
Clementi, Maria E., Roberto Scatena, Alvaro Mordente, Saverio G. Condò, Massimo Castagnola und Bruno Giardina. „Oxygen Transport by Fetal Bovine Hemoglobin“. Journal of Molecular Biology 255, Nr. 1 (Januar 1996): 229–34. http://dx.doi.org/10.1006/jmbi.1996.0019.
Salzano, A. M., A. Pauciullo, D. Ambrosio C, G. Novi, M. Strazzullo und 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 (15.07.2016): 145–51. http://dx.doi.org/10.17221/8128-cjas.
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, Nr. 1 (31.10.2016): 252–60. http://dx.doi.org/10.1002/btpr.2380.
D'Agnillo, Felice. „Redox active hemoglobin enhances lipopolysaccharide-induced injury to cultured bovine endothelial cells“. American Journal of Physiology-Heart and Circulatory Physiology 287, Nr. 4 (Oktober 2004): H1875—H1882. http://dx.doi.org/10.1152/ajpheart.00164.2004.
Condò, Saverio G., Said El-Sherbini und Bruno Giardina. „Temperature modulation of bovine hemoglobins“. Biochemical and Biophysical Research Communications 177, Nr. 3 (Juni 1991): 956–62. http://dx.doi.org/10.1016/0006-291x(91)90631-g.
Lasne, Françoise, Nathalie Crepin, Michael Ashenden, Michel Audran und Jacques de Ceaurriz. „Detection of Hemoglobin-Based Oxygen Carriers in Human Serum for Doping Analysis: Screening by Electrophoresis“. Clinical Chemistry 50, Nr. 2 (01.02.2004): 410–15. http://dx.doi.org/10.1373/clinchem.2003.026583.
Dang, Meng, Qiliang Deng, Guozhen Fang, Dongdong Zhang, Jingmin Liu und Shuo Wang. „Preparation of novel anionic polymeric ionic liquid materials and their potential application to protein adsorption“. Journal of Materials Chemistry B 5, Nr. 31 (2017): 6339–47. http://dx.doi.org/10.1039/c7tb01234a.
Marta, Maurizio, Maria Patamia, Alessandro Lupi, Mirca Antenucci, Mario Di Iorio, Sergio Romeo, Raffaele Petruzzelli, Massimo Pomponi und Bruno Giardina. „Bovine Hemoglobin Cross-Linked through the Chains“. Journal of Biological Chemistry 271, Nr. 13 (29.03.1996): 7473–78. http://dx.doi.org/10.1074/jbc.271.13.7473.
Cempel, Nathalie, Didier Guillochon und Jean-Marie Piot. „Preparation of Photodynamic Hydrolyzates from Bovine Hemoglobin“. Journal of Agricultural and Food Chemistry 42, Nr. 9 (September 1994): 2059–63. http://dx.doi.org/10.1021/jf00045a042.
Maghraby, Ahmed Mohamed, und Maha Anwar Ali. „Spectroscopic study of gamma irradiated bovine hemoglobin“. Radiation Physics and Chemistry 76, Nr. 10 (Oktober 2007): 1600–1605. http://dx.doi.org/10.1016/j.radphyschem.2007.01.008.
Daoud, Rachid, Veronique Dubois, Loredana Bors-Dodita, Naima Nedjar-Arroume, Francois Krier, Nour-Eddine Chihib, Patrice Mary, Mostafa Kouach, Gilbert Briand und Didier Guillochon. „New antibacterial peptide derived from bovine hemoglobin“. Peptides 26, Nr. 5 (Mai 2005): 713–19. http://dx.doi.org/10.1016/j.peptides.2004.12.008.
Trujillo, Edward M. „Osmotic pressure measurements of dissociating bovine hemoglobin“. Journal of Membrane Science 69, Nr. 3 (Mai 1992): 213–22. http://dx.doi.org/10.1016/0376-7388(92)80040-q.
Outman, Ahlam, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Bernard Gressier, Bruno Eto und 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, Nr. 15 (25.07.2023): 11921. http://dx.doi.org/10.3390/ijms241511921.
Marva, E., und RP Hebbel. „Denaturing interaction between sickle hemoglobin and phosphatidylserine liposomes“. Blood 83, Nr. 1 (01.01.1994): 242–49. http://dx.doi.org/10.1182/blood.v83.1.242.242.
Marva, E., und RP Hebbel. „Denaturing interaction between sickle hemoglobin and phosphatidylserine liposomes“. Blood 83, Nr. 1 (01.01.1994): 242–49. http://dx.doi.org/10.1182/blood.v83.1.242.bloodjournal831242.
Maas, Bart H. A., Anneke Buursma, Rob A. J. Ernst, Anton H. J. Maas und Willem G. Zijlstra. „Lyophilized bovine hemoglobin as a possible reference material for the determination of hemoglobin derivatives in human blood“. Clinical Chemistry 44, Nr. 11 (01.11.1998): 2331–39. http://dx.doi.org/10.1093/clinchem/44.11.2331.
Outman, Ahlam, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Jihen Dhaouefi, Bernard Gressier, Bruno Eto und 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, Nr. 17 (22.08.2023): 13055. http://dx.doi.org/10.3390/ijms241713055.
Asmari, Abdulrahman K. Al. „Gastric antisecretory and antiulcer activity of bovine hemoglobin“. World Journal of Gastroenterology 19, Nr. 21 (2013): 3291. http://dx.doi.org/10.3748/wjg.v19.i21.3291.
Hu, Tao, Dongxia Li und Zhiguo Su. „Preparation and Characterization of Dimeric Bovine Hemoglobin Tetramers“. Journal of Protein Chemistry 22, Nr. 5 (Juli 2003): 411–16. http://dx.doi.org/10.1023/b:jopc.0000005455.94103.b8.
Nedjar-Arroume, Naïma, Véronique Dubois-Delval, Estelle Yaba Adje, Jonathan Traisnel, François Krier, Patrice Mary, Mostafa Kouach, Gilbert Briand und Didier Guillochon. „Bovine hemoglobin: An attractive source of antibacterial peptides“. Peptides 29, Nr. 6 (Juni 2008): 969–77. http://dx.doi.org/10.1016/j.peptides.2008.01.011.
Zhang, Hong-Mei, Yan-Qing Wang, Qiu-Hua Zhou und Guang-Li Wang. „Molecular interaction between phosphomolybdate acid and bovine hemoglobin“. Journal of Molecular Structure 921, Nr. 1-3 (März 2009): 156–62. http://dx.doi.org/10.1016/j.molstruc.2008.12.049.
Gotshall, Robert W., Karyn L. Hamilton, Benjamin Foreman, Martha C. Tissot van Patot und David C. Irwin. „Glutaraldehyde-polymerized bovine hemoglobin and phosphodiesterase-5 inhibition*“. Critical Care Medicine 37, Nr. 6 (Juni 2009): 1988–93. http://dx.doi.org/10.1097/ccm.0b013e3181a00597.
Ge, Moyan, Yi Shen, Weiming Chen, Yaotian Peng und Ziyan Pan. „Adsorption of Bovine Hemoglobin by Sulfonated Polystyrene Nanospheres“. ChemistrySelect 4, Nr. 10 (08.03.2019): 2874–80. http://dx.doi.org/10.1002/slct.201803780.
Chi, Zhenxing, Rutao Liu, Bingjun Yang und Hao Zhang. „Toxic interaction mechanism between oxytetracycline and bovine hemoglobin“. Journal of Hazardous Materials 180, Nr. 1-3 (15.08.2010): 741–47. http://dx.doi.org/10.1016/j.jhazmat.2010.04.110.
Soma, Lawrence R., Cornelius E. Uboh, Fuyu Guan, Yi Luo, Peter J. Moate, Raymond C. Boston und Bernd Driessen. „The Pharmacokinetics of Hemoglobin-Based Oxygen Carrier Hemoglobin Glutamer-200 Bovine in the Horse“. Anesthesia & Analgesia 100, Nr. 6 (Juni 2005): 1570–75. http://dx.doi.org/10.1213/01.ane.0000154081.38466.09.
Soma, LR, F. Guan, CE Uboh, Y. Luo, PJ Moate und B. Driessen. „Pharmacokinetics of hemoglobin-based oxygen carrier hemoglobin-glutamer-200 bovine (oxyglobin) in the horse“. Veterinary Anaesthesia and Analgesia 32, Nr. 4 (Juli 2005): 17. http://dx.doi.org/10.1111/j.1467-2995.2005.00232a_35.x.
Gasthuys, Maryline, Sandra Alves und Jean-Claude Tabet. „N-Terminal Adducts of Bovine Hemoglobin with Glutaraldehyde in a Hemoglobin-Based Oxygen Carrier“. Analytical Chemistry 77, Nr. 10 (Mai 2005): 3372–78. http://dx.doi.org/10.1021/ac048107i.
Lurie, Fedor, Jonathan S. Jahr und 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, Nr. 4 (Oktober 2002): 870–73. http://dx.doi.org/10.1213/00000539-200210000-00014.
Lurie, Fedor, Jonathan S. Jahr und 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, Nr. 4 (Oktober 2002): 870–73. http://dx.doi.org/10.1097/00000539-200210000-00014.
Nogueira, Nadir N., Célia Colli und 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, Nr. 4 (Dezember 1992): 459–65. http://dx.doi.org/10.1590/s0102-311x1992000400011.
Abou-Diab, Mira, Jacinthe Thibodeau, Ismail Fliss, Pascal Dhulster, Laurent Bazinet und 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, Nr. 5 (11.05.2022): 512. http://dx.doi.org/10.3390/membranes12050512.
Maity, Mritunjoy, Sandip Dolui und 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, Nr. 46 (2015): 31216–27. http://dx.doi.org/10.1039/c5cp04661k.
Williams, Alexander T., Alfredo Lucas, Cynthia R. Muller, Crystal Bolden-Rush, Andre F. Palmer und Pedro Cabrales. „Balance between oxygen transport and blood rheology during resuscitation from hemorrhagic shock with polymerized bovine hemoglobin“. Journal of Applied Physiology 129, Nr. 1 (01.07.2020): 97–107. http://dx.doi.org/10.1152/japplphysiol.00016.2020.
Outman, Ahlam, Mohamed Bouhrim, Codjo Hountondji, Omar M. Noman, Ali S. Alqahtani, Bernard Gressier, Naïma Nedjar und Bruno Eto. „Obtaining New Candidate Peptides for Biological Anticancer Drugs from Enzymatic Hydrolysis of Human and Bovine Hemoglobin“. International Journal of Molecular Sciences 24, Nr. 20 (19.10.2023): 15383. http://dx.doi.org/10.3390/ijms242015383.
Das, Sourav, Nikita Bora, Mostofa Ataur Rohman, Raju Sharma, Anupam Nath Jha und 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, Nr. 33 (2018): 21668–84. http://dx.doi.org/10.1039/c8cp02760a.
Sheffield, CL, und JR DeLoach. „Preparation and in vivo evaluation of two bovine hemoglobin‐based plasma expanders“. Biotechnology and Applied Biochemistry 12, Nr. 6 (Dezember 1990): 630–42. http://dx.doi.org/10.1111/j.1470-8744.1990.tb00137.x.
Zhang, Zhifeng, Wenwen Wang, Zhentan Lu, Ke Liu, Qiongzhen Liu und 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, Nr. 11 (2018): 8537–43. http://dx.doi.org/10.1039/c8nj00198g.
Bu, Fengrong, Heyao Wang und Xiaoxia Zhu. „Studies on the Resuscitative Efficacy of Polymerized Bovine Hemoglobin“. Artificial Cells, Blood Substitutes, and Biotechnology 28, Nr. 6 (2000): 493–501. http://dx.doi.org/10.3109/10731190009139266.
Bucci, Enrico, Clara Fronticelli, Charles Orth, Maria Cristina Martorana, Luisa Aebischer und Pasquale Angeloni. „Bovine Hemoglobin as a Basis for Artificial Oxygen Carriers“. Biomaterials, Artificial Cells and Artificial Organs 16, Nr. 1-3 (Januar 1988): 197–204. http://dx.doi.org/10.3109/10731198809132569.
Bradley, R., S. Sloshberg, K. Nho, B. Czuba, D. Szesko und R. Shorr. „Production of Peg-Modified Bovine Hemoglobin: Economics and Feasibility“. Artificial Cells, Blood Substitutes, and Biotechnology 22, Nr. 3 (Januar 1994): 657–67. http://dx.doi.org/10.3109/10731199409117896.
Ouellet, H., Y. Ouellet, C. Richard, M. Labarre, B. Wittenberg, J. Wittenberg und M. Guertin. „Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide“. Proceedings of the National Academy of Sciences 99, Nr. 9 (16.04.2002): 5902–7. http://dx.doi.org/10.1073/pnas.092017799.
Li, Sha, Hongyuan Shang, Fasheng Liu, Min Ma und Aiping Zhang. „Toxic effects of copper (II) ions on bovine hemoglobin“. Spectroscopy Letters 51, Nr. 2 (07.02.2018): 67–73. http://dx.doi.org/10.1080/00387010.2017.1335754.
Bu, Fengrong, Heyao Wang und Xiaoxia Zhu. „Studies on the Resuscitative Efficacy of Polymerized Bovine Hemoglobin“. Artificial Cells, Blood Substitutes, and Biotechnology 28, Nr. 6 (Januar 2000): 493–501. http://dx.doi.org/10.1080/10731190009139266.