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Journal articles on the topic 'Bovine hemoglobin'

Author: Grafiati

Published: 18 May 2024

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1

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.

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2

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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3

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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4

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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5

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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6

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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7

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.

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8

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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9

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.

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10

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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11

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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12

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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13

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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14

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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15

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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16

Outman, Ahlam, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Bernard Gressier, Bruno Eto, and 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, no. 15 (July 25, 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.

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17

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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18

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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19

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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20

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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21

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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22

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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23

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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24

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.

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25

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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26

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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27

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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28

Outman, Ahlam, Barbara Deracinois, Christophe Flahaut, Mira Abou Diab, Jihen Dhaouefi, Bernard Gressier, Bruno Eto, and 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, no. 17 (August 22, 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.

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29

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.

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30

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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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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32

Romito, Bryan T., Mandy M. McBroom, Dawn Bryant, Jacob Gamez, Akeel Merchant, and Steven E. Hill. "The effect of SANGUINATE® (PEGylated carboxyhemoglobin bovine) on cardiopulmonary bypass functionality using a bovine whole blood model of normovolemic hemodilution." Perfusion 35, no. 1 (May 30, 2019): 19–25. http://dx.doi.org/10.1177/0267659119850681.

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Background: Cardiac surgery using cardiopulmonary bypass carries a high risk of bleeding and need for blood transfusion. Blood administration is associated with increased rates of morbidity and mortality. Perioperatively, strategies are often employed to reduce blood transfusions in high-risk patients or in situations where blood transfusion is contraindicated. Normovolemic hemodilution is a blood conservation technique used during cardiac surgery that involves replacement of blood with fluids. SANGUINATE® (PEGylated carboxyhemoglobin bovine) is a novel hemoglobin-based oxygen carrier that can deliver oxygen effectively to tissues in the presence of severe hypoxia. The use of a hemoglobin-based oxygen carrier during hemodilution may augment tissue oxygen delivery and reduce blood transfusion. Methods: Six standardized cardiopulmonary bypass runs simulating normovolemic hemodilution using varying proportions of bovine whole blood and SANGUINATE were performed. Pump speed, flow rate, line pressures, hemoglobin concentration, oxygenation, and degree of anticoagulation were assessed at regular intervals. Membrane oxygenators and arterial line filters were inspected for evidence of clotting following each run. Results: Increases in the pressure drop across the membrane oxygenator were detected during runs 5 and 6. Median activated clotting time values were able to be maintained at goal during the runs, and SANGUINATE did not appear to be thrombogenic. Hemoglobin concentration decreased following the addition of SANGUINATE. Oxygenation was maintained during all runs that included SANGUINATE. Conclusion: SANGUINATE does not impact the performance of the cardiopulmonary bypass circuit in a bovine whole blood model. The results support further evaluation of SANGUINATE in the setting of normovolemic hemodilution and cardiopulmonary bypass.

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33

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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34

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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35

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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36

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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37

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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38

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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39

FRONTICELLI, Clara, Enrico BUCCI, Anna RAZYNSKA, Joanna SZNAJDER, Barbara URBAITIS, and Zygmunt GRYCZYNSKI. "Bovine hemoglobin pseudo-crosslinked with mono(3,5-dibromosalicyl)-fumarate." European Journal of Biochemistry 193, no. 2 (October 1990): 331–36. http://dx.doi.org/10.1111/j.1432-1033.1990.tb19342.x.

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40

Froidevaux, R., F. Krier, N. Nedjar-Arroume, D. Vercaigne-Marko, E. Kosciarz, C. Ruckebusch, P. Dhulster, and D. Guillochon. "Antibacterial activity of a pepsin-derived bovine hemoglobin fragment." FEBS Letters 491, no. 1-2 (February 20, 2001): 159–63. http://dx.doi.org/10.1016/s0014-5793(01)02171-8.

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41

Dimino, Michael L., and Andre F. Palmer. "Purification of bovine hemoglobin via fast performance liquid chromatography." Journal of Chromatography B 856, no. 1-2 (September 2007): 353–57. http://dx.doi.org/10.1016/j.jchromb.2007.05.040.

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42

Webster, Kyle D., Dana Dahhan, Abigail M. Otto, Cheyanne L. Frosti, William L. Dean, Jonathan B. Chaires, and Kenneth W. Olsen. "“Inside-Out” PEGylation of Bovine β-Cross-Linked Hemoglobin." Artificial Organs 41, no. 4 (March 20, 2017): 351–58. http://dx.doi.org/10.1111/aor.12928.

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Wang, Yan-Qing, Hong-Mei Zhang, Gen-Cheng Zhang, Shuang-Xia Liu, Qiu-Hua Zhou, Zheng-Hao Fei, and Zong-Tang Liu. "Studies of the interaction between paraquat and bovine hemoglobin." International Journal of Biological Macromolecules 41, no. 3 (August 2007): 243–50. http://dx.doi.org/10.1016/j.ijbiomac.2007.02.011.

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Wang, Yan-Qing, Hong-Mei Zhang, and Qiu-Hua Zhou. "Studies on the interaction of caffeine with bovine hemoglobin." European Journal of Medicinal Chemistry 44, no. 5 (May 2009): 2100–2105. http://dx.doi.org/10.1016/j.ejmech.2008.10.010.

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Hu, Tao, and Zhiguo Su. "A solid phase adsorption method for preparation of bovine serum albumin–bovine hemoglobin conjugate." Journal of Biotechnology 100, no. 3 (February 2003): 267–75. http://dx.doi.org/10.1016/s0168-1656(02)00246-8.

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Wahab, Rizwan, Sourabh Dwivedi, Mohd Shahnawaz Khan, Abdulrahman M. Al-Senaidy, Hyung-Shik Shin, Javed Musarrat, and Abdulaziz A. Al-Khedhairy. "Optical Analysis of Zinc Oxide Quantum Dots with Bovine Serum Albumin and Bovine Hemoglobin." Journal of Pharmaceutical Innovation 9, no. 1 (February 16, 2014): 48–52. http://dx.doi.org/10.1007/s12247-014-9174-5.

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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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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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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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Abstract:

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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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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