The distribution of readily reducible disulphide bonds in wool
- 1 May 1961
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 79 (2) , 280-286
- https://doi.org/10.1042/bj0790280
Abstract
Wool was reduced between 6 and 60% at pH 5.0 with mercaptoacetate, alkylated with [2-C14]iodoacetate and fractionally extracted with alkaline mercaptoacetate. After alkylation with unlabelled iodoacetate these fractions were separated by acid precipitation into proteins of high- and low-sulphur content. The extent of reduction at pH 5.0 in each constituent was determined by isolating the S-carboxy-methylcysteine and measuring its specific radioactivity. The disulphide bonds in the proteins of high- and low-sulphur content from any particular fraction were reduced to the same extent. Variations between the fractions themselves were quite small, usually less than 5% and not . deviating by more than 10% from the mean. It was concluded that the cystine residues of the so-called (A+B) fraction are not confined to any particular protein component and it is inferred that they are equally distributed throughout the morphological components of wool. The apparent differences in reactivity between disulphide bonds in wool have been interpreted as resulting from an equilibrium between the SS-SH system and the reducing agents used.Keywords
This publication has 20 references indexed in Scilit:
- A MODIFIED NINHYDRIN REAGENT FOR THE PHOTOMETRIC DETERMINATION OF AMINO ACIDS AND RELATED COMPOUNDSPublished by Elsevier ,2021
- Appendix—The equilibrium between the disulphide bonds in wool and mercaptoacetateBiochemical Journal, 1961
- The reaction of the disulphide groups of insulin with sodium sulphiteBiochemical Journal, 1960
- Changes in the reactivity of disulfide bonds in bovine serum albumin on denaturationArchives of Biochemistry and Biophysics, 1960
- The relationship between the chemical heterogenity of wool keratin and the mode of incorporation of the cystine residuesBiochimica et Biophysica Acta, 1959
- Stoichiometry in the estimation of disulphide in intact proteins using mercuric chlorideBiochimica et Biophysica Acta, 1959
- The reactivity of the cystine linkages in wool towards reducing agentsBiochemical Journal, 1955
- The reactivity of the combined cystine of proteins other than woolBiochemical Journal, 1948
- The action of sulphites on the cystine disulphide linkages of woolBiochemical Journal, 1942
- The action of sulphites on the cystine disulphide linkages in woolBiochemical Journal, 1938