Isolation of the smallest component of silk protein

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 w...

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Bibliographic Details
Published in:Biochemical journal 1980-05, Vol.187 (2), p.413-417
Main Author: Tokutake, S
Format: Article
Language:English
Subjects:
Amino Acids - analysis
Animals
Bombyx - analysis
Bombyx mori
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Fibroins - isolation & purification
Mercaptoethanol
Peptides, Cyclic - isolation & purification
Sericins
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Summary: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.
ISSN:0306-3275
0264-6021
1470-8728
DOI:10.1042/bj1870413