TY - JOUR
T1 - Proteomic studies of isoforms of the P25 component of Bombyx mori fibroin
AU - Zhang, Pingbo
AU - Yamamoto, Kohji
AU - Aso, Yoichi
AU - Banno, Yutaka
AU - Sakano, Daisuke
AU - Wang, Yongqiang
AU - Fujii, Hiroshi
N1 - Funding Information:
This work was supported in part by the National Bioresource Project (Silkworm) from the Ministry of Education, Science, and Culture of Japan.
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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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U2 - 10.1271/bbb.69.2086
DO - 10.1271/bbb.69.2086
M3 - Article
C2 - 16306689
AN - SCOPUS:28244488657
SN - 0916-8451
VL - 69
SP - 2086
EP - 2093
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 11
ER -