title: Isolation of three main sericin components from the cocoon of the silkworm, Bombyx mori.
abstract: To characterize the sericin components of the cocoon of silkworm Bombyx mori, fresh cocoon shells were dissolved in saturated aqueous lithium thiocyanate containing 2-mercaptoethanol, and fractionated by ethanol precipitation. Cocoon sericin was found to mainly consist of three polypeptides having molecular masses of the 400, 250, and 150 kDa estimated by SDS-PAGE, which corresponds to the sericin present in the middle, anterior, and posterior part of the middle silk gland. The amino acid compositions of the 400 and 150 kDa components were similar to each other, but that of the 250 kDa component was different. This suggests differences in the coding gene and properties of the 250 kDa sericin from the other two.
authors.affiliation: National Institute of Agrobiological Sciences, Owashi 1-2, Tsukuba, Ibaraki 305-8634, Japan. takasu@affrc.go.jp
authors.forename: Yoko
authors.initials: Y
authors.lastname: Takasu
authors.forename: Hiromi
authors.initials: H
authors.lastname: Yamada
authors.forename: Kozo
authors.initials: K
authors.lastname: Tsubouchi
mesh_terms: D000818:Animals; D012831:Bombyx / Q000737:chemistry* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D019476:Insect Proteins / Q000032:analysis / Q000737:chemistry; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis / Q000737:chemistry; D010456:Peptides, Cyclic / Q000032:analysis* / Q000737:chemistry*; D047030:Sericins
chemical_list: D019476:Insect Proteins; D010455:Peptides; D010456:Peptides, Cyclic; D047030:Sericins