PMID: 9189827Jun 15, 1997Paper

Studies on the desamidation of bovine collagen

Journal of Biomedical Materials Research
M Radhika, P K Sehgal

Abstract

The most important reactive groups in collagen are amino, amido, guanidino, and carboxyl, all of which are present in comparatively large numbers. It is possible to modify amide groups present in the collagen of achilles tendons and hide trimmings by desamidation (DAM). DAM causes progressive hydrolysis of the amide groups of asparagine and glutamine side chains of collagen, thereby resulting in the reduction of the amide content of collagen. Loss of amide brings about an increase in the number of free carboxyl groups in the desamidated collagen, shown by reduction in its isoionic pH. The new modified collagen, like type I bovine collagen, has high viscosity and high hydroxyproline content. The fibril formation of the modified collagen showed slight variation, and polyacrylamide gel electrophoretic analysis indicated largely alpha components, indicating destruction of inter- and intramolecular crosslinks. The swelling behavior of the modified collagen is significantly higher compared to type I bovine collagen.

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Citations

Sep 14, 2000·Journal of Biomedical Materials Research·A CurodeauS Caldarise
Jul 13, 2002·Journal of Biomedical Materials Research·Baek-Hee LeeKyu Hwan Lee
Jan 5, 2002·Biomaterials·Lenaldo B RochaMarcos A Rossi
Jan 6, 2000·Comparative Biochemistry and Physiology. Part C, Pharmacology, Toxicology & Endocrinology·M RadhikaP K Sehgal
Mar 20, 2019·Biomedical Engineering Online·Michael Meyer
Apr 10, 2016·Journal of Biomedical Materials Research. Part a·Shirin ToosiJavad Behravan

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