Abstract
A soluble fraction of alpha-keratin was obtained on fission of disulphide bonds. The fraction was soluble in the oxidizing solution and would normally be lost when such procedures are used for isolating keratose fractions. This fraction, which constituted 6% by weight of keratin, was rich in cystine, and about 30% of the fraction had a mol.wt. of less than 20 000.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
43 articles.
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