Studies on silk fibroin of Bombyx mori. I. Fractionation of fibroin prepared from the posterior silk gland.

Abstract:

:1. Fractionation of fibroin prepared from the posterior silk glands of Bombyx mori was carried out. After carboxymethylation of the fibroin, it was fractionated by ammonium sulfate precipitation, Sephadex G-200 gel filtration and DEAE-cellulose column chromatography. 2. The fibroin was composed of at least two protein groups of large molecular size and three or four components of small molecular size, and, in addition, a mixture of proteins ranging in size from about 25,000 to more than 100,000 daltons with almost the same amino acid compositions. 3. The latter proteins contained about 48% glycine, 32% alanine, 11% serine, 4.5% tyrosine, 2% valine, and other minor amino acids. The sum of these main five amino acids accounts for more than 97% of the total amino acid residues of the proteins. 4. The present results indicate major heterogeneity in the molecular size of posterior silk gland fibroin, and, in addition, suggest the possibility of repeating sequences with relatively simple amino acid compositions in major peptide chains of fibroin.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Shimura K,Kikuchi A,Ohtomo K,Katagata Y,Hyodo A

doi

10.1093/oxfordjournals.jbchem.a131328

keywords:

subject

Has Abstract

pub_date

1976-10-01 00:00:00

pages

693-702

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

80

pub_type

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