The Bombyx mori silk proteins: characterization of large polypeptides.
Proteins taken directly from the Bombyx mori silk gland have been separated and identified as either fibroin or sericin on the basis of their location within the gland and their amino acid composition. Molecular weights of these polypeptides have been determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and by agarose-guanidine chromatography. Fibroin consists of approximately equimolar amounts of two large (350,000) polypeptide chains. These may be the products of distinct fibroin alleles present in hybrid silkworm strains. Sericin, on the other hand, is composed of at least the three largest polypeptides (130,000-220,000) present in a mixture of proteins ranging in size from about 20,000 to 220,000.
D000483:Alleles; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D012831:Bombyx / Q000032:analysis* / Q000378:metabolism; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005349:Fibroins / Q000032:analysis / Q000096:biosynthesis; D006824:Hybridization, Genetic; D046911:Macromolecular Substances; D008970:Molecular Weight; D014176:Protein Biosynthesis; D011506:Proteins / Q000032:analysis
D000596:Amino Acids; D046911:Macromolecular Substances; D011506:Proteins; D005349:Fibroins