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. 1980 May 1;187(2):413–417. doi: 10.1042/bj1870413

Isolation of the smallest component of silk protein.

S Tokutake
PMCID: PMC1161807  PMID: 7396855

Abstract

Silk proteins were solubilized from cocoons with ethylenediamine/cupric hydroxide solution. A series of polymers of the smallest component, detected by polyacrylamide-gel electrophoresis, could be converted into the smallest component by reduction and aminoethylation. Fibroin and sericin fractions were separated by precipitation of sericin at pH 5.5. On gel electrophoresis, sericin showed distinct bands but fibroin did not. The components of fibroin and sericin were fractionated by gel filtration on Sepharose 6B. The smallest component in the sericin fraction was purified by rechromatography and showed a single band on gel electrophoresis. Its mol. wt. was 24 000, and its amino acid composition was determined.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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