The effect of deamination and esterification on the reactivity of collagen
- 1 January 1949
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 44 (2) , 142-152
- https://doi.org/10.1042/bj0440142
Abstract
Collagen was deaminated with nitrous acid and esterified with methyl sulfate and methyl bromide, and the effect of these treatments on the reactivity of collagen towards acids, bases, tannins, chromium and formaldehyde determined. Modification of the guanidino groups by treatment with hypochlorite was only partially successful; only 40-50% of the arginine was destroyed and there was extensive general breakdown of the collagen. It is suggested that combination of tannins is related to the positive charge carried by the collagen, combination of chromium involves co-ordination of both amino and carboxyl groups of the collagen with the same chromium complex, and combination with formaldehyde occurs mainly with the amino and guanidino groups. Increase in the thermal stability results only from combination of formaldehyde with amino groups.Keywords
This publication has 10 references indexed in Scilit:
- The amino-acid composition and titration curve of collagenBiochemical Journal, 1948
- The effect of alkalis on collagenBiochemical Journal, 1948
- The isolation of hydroxylysine picrate from a gelatin hydrolysateBiochemical Journal, 1948
- Specific Group Reagents for Proteins.Chemical Reviews, 1947
- Studies on bacterial amino-acid decarboxylasesBiochemical Journal, 1945
- Experiments on the methylation and acetylation of wool, silk fibroin, collagen and gelatinBiochemical Journal, 1944
- The methylation of wool with methyl sulphate and methyl halidesBiochemical Journal, 1941
- The determination of small amounts of dimethylamine in biological fluidsBiochemical Journal, 1938
- The Analysis of Proteins. II. The Action of Nitrous Acid upon the Hexone BasesBiochemical Journal, 1924
- The Action of Diazomethane on CaseinogenBiochemical Journal, 1914