文献类型: 外文期刊
作者: Zhang, PB 1 ; Yamamoto, K 2 ; Aso, Y 2 ; Banno, Y 2 ; Sakano, D 2 ; Wang, YQ 2 ; Fujii, H 3 ;
作者机构: 1.Kyushu Univ, Inst Genet Resources, Fukuoka 8128581, Japan
2.Kyushu Univ, Inst Genet Resources, Fukuoka 8128581, Japan; Kyushu Univ, Fac Agr, Fukuoka 8128581, Japan; Zhejiang Acad Agr Sci, Hangzhou 310021, Peoples R China
3.Kyushu Univ, Inst Genet Resources, Fukuoka 8128581, Japan; Kyushu Univ, Fac Agr, Fukuoka 8128581, Japan; Zhejiang Acad Agr Sci, Hangzhou 310021, Peoples R
关键词: proteomics;silkworm;P25 isoform;fibroin
期刊名称:BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY ( 影响因子:2.043; 五年影响因子:2.017 )
ISSN: 0916-8451
年卷期: 2005 年 69 卷 11 期
页码:
收录情况: SCI
摘要: It is recognized that P25 is one of three polypeptide components of the fibroin synthesized in the larval silk gland (SG) of silkworm, having two glycosylated isoforms. In the present study, however, eight P25 isoforms were separated by proteomics, including two-dimensional gel electrophoresis of whole SG proteins, and were identified by the peptide mass fingerprinting method. Four of the eight isoforms were identified as Bombyx mandarina P25s, although the SG of Bombyx mori has never been considered to contain the P25 from B. mandarina. It is suggested that this diversity of P25 isoforms depends on phosphorylation modification in addition to glycosylation.
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