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The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species.
Abstract: The effect of trypsin digestion on iron-saturated and iron-free (apo) human, rabbit, bovine, pig and horse tranferrins has been studied. Iron-binding fragments were produced only from iron-saturated pig and bovine transferrins although some cleavage of the polypeptide chain occurred in all cases. The apo-transferrins were generally degraded to a greater extent than the corresponding iron-saturated proteins. The ability of the different transferrins to donate iron to rabbit reticulocytes varied in the order rabbit approximately pig greater than human approximately horse greater than bovine. Trypsin digestion considerably reduced the ability of pig and bovine transferrins to donate iron to rabbit reticulocytes, slightly reduced the iron-donating ability of rabbit transferrin, and had almost no effect on that of human or horse transferrins.
Publication Date: 1980-04-25 PubMed ID: 7378455DOI: 10.1016/0005-2795(80)90040-9Google Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Comparative Study
- Journal Article
Summary
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This research article explores how trypsin digestion influences the structure and iron-donating properties of transferrins from various species, including humans, rabbits, cows, pigs, and horses. The results reveal that the impact of trypsin digestion on the capacity of these transferrins to deliver iron to rabbit red blood cells varies depending on the species in question.
Study on the Impact of Trypsin Digestion
- The research sought to examine the effects of trypsin digestion on iron-saturated and iron-free transferrins from humans, rabbits, cows, pigs, and horses. Trypsin is a digestive enzyme that breaks down proteins in the digestive system.
- Iron-binding fragments were only produced from iron-saturated pig and bovine transferrins. This indicates that these two types of transferrins underwent some level of cleavage of the polypeptide chain, an important component of protein structure.
- On the other hand, the experiments showed that all the apo-transferrins – transferrins without bound iron – were generally degraded more than their iron-saturated counterparts. This could potentially suggest differing levels of stability between iron-free and iron-saturated transferrins.
Variation in Iron-Donation Ability
- Another key aspect of the research was to analyze the ability of the different transferrins to donate iron to rabbit reticulocytes, immature red blood cells. The findings revealed a particular order among the species: rabbit and pig transferrins showed the highest ability, followed by human and horse transferrins, while bovine transferrin had the least ability.
- The effects of trypsin digestion on these abilities were also variable. Trypsin digestion greatly reduced the capacity of pig and bovine transferrins to donate iron, slightly reduced that of the rabbit transferrin, and had almost negligible impact on the human and horse transferrins.
- These variations may be attributable to differences in the biochemical structures or sensitivities of the transferrins among these species. More research would be needed to confirm and further investigate these findings.
Cite This Article
APA
Esparza I, Brock JH.
(1980).
The effect of trypsin digestion on the structure and iron-donating properties of transferrins from several species.
Biochim Biophys Acta, 622(2), 297-307.
https://doi.org/10.1016/0005-2795(80)90040-9 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Apoproteins / blood
- Binding Sites
- Cattle
- Horses
- Humans
- In Vitro Techniques
- Iron / blood
- Kinetics
- Peptide Fragments / blood
- Rabbits
- Reticulocytes / metabolism
- Species Specificity
- Swine
- Transferrin / metabolism
- Trypsin
Citations
This article has been cited 14 times.- Long H, Yu QX. Studies on resistance characteristic and cDNA sequence conservation of transferrin from crucian carp, Carassius auratus. Mol Cell Biochem 2007 Sep;303(1-2):201-9.
- van Rensburg SJ, van Zyl J, Hon D, Daniels W, Hendricks J, Potocnik F, Erasmus R. Biochemical model for inflammation of the brain: the effect of iron and transferrin on monocytes and lipid peroxidation. Metab Brain Dis 2004 Jun;19(1-2):97-112.
- Hissen AH, Chow JM, Pinto LJ, Moore MM. Survival of Aspergillus fumigatus in serum involves removal of iron from transferrin: the role of siderophores. Infect Immun 2004 Mar;72(3):1402-8.
- Miller RA, Britigan BE. Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 1997 Jan;10(1):1-18.
- Miller RA, Rasmussen GT, Cox CD, Britigan BE. Protease cleavage of iron-transferrin augments pyocyanin-mediated endothelial cell injury via promotion of hydroxyl radical formation. Infect Immun 1996 Jan;64(1):182-8.
- Britigan BE, Hayek MB, Doebbeling BN, Fick RB Jr. Transferrin and lactoferrin undergo proteolytic cleavage in the Pseudomonas aeruginosa-infected lungs of patients with cystic fibrosis. Infect Immun 1993 Dec;61(12):5049-55.
- Wolz C, Hohloch K, Ocaktan A, Poole K, Evans RW, Rochel N, Albrecht-Gary AM, Abdallah MA, Döring G. Iron release from transferrin by pyoverdin and elastase from Pseudomonas aeruginosa. Infect Immun 1994 Sep;62(9):4021-7.
- Miller RA, Britigan BE. Protease-cleaved iron-transferrin augments oxidant-mediated endothelial cell injury via hydroxyl radical formation. J Clin Invest 1995 Jun;95(6):2491-500.
- Osterloh K, Forth W. Determination of transferrin-like immunoreactivity in the mucosal homogenate of the duodenum, jejunum, and ileum of normal and iron deficient rats. Blut 1981 Oct;43(4):227-35.
- Brock JH. The effect of iron and transferrin on the response of serum-free cultures of mouse lymphocytes to concanavalin A and lipopolysaccharide. Immunology 1981 Jun;43(2):387-92.
- Heaphy S, Williams J. The preparation and partial characterization of N-terminal and C-terminal iron-binding fragments from rabbit serum transferrin. Biochem J 1982 Sep 1;205(3):611-7.
- Trebichavský I, Macků B, Viklický V, Koukal M, Siman P. Monoclonal antibodies against pig transferrin. Blocking and binding activity. Folia Microbiol (Praha) 1987;32(5):448-52.
- Brock JH, Mainou-Fowler T, Webster LM. Evidence that transferrin may function exclusively as an iron donor in promoting lymphocyte proliferation. Immunology 1986 Jan;57(1):105-10.
- Britigan BE, Edeker BL. Pseudomonas and neutrophil products modify transferrin and lactoferrin to create conditions that favor hydroxyl radical formation. J Clin Invest 1991 Oct;88(4):1092-102.
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