Proteomic studies of isoforms of the P25 component of Bombyx mori fibroin

Pingbo Zhang, Kohji Yamamoto, Yoichi Aso, Yutaka Banno, Daisuke Sakano, Yongqiang Wang, Hiroshi Fujii

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)2086-2093
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Issue number11
Publication statusPublished - 2005

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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