Abstract
The silk gland of Bombyx mori is an organ specialized for the synthesis and secretion of silk proteins. We report here the resolution of silk gland proteins by 2-DE and the identification of many of those proteins. This was accomplished by dissecting the glands into several sections, with each exhibiting more than 400 protein spots by 2-DE, of which 100 spots were excised and characterized by in-gel digestion followed by PMF. Ninety-three proteins were tentatively identified. These were then categorized into groups involved in silk protein secretion, transport, lipid metabolism, defense, etc. Western blotting of a 2-DE gel using an antibody of the carotenoid binding protein confirmed the presence of this protein in the silk gland. Proteins including fibroin L-chain and P25 were found as multiple isoforms, some of which contained differential amounts of phosphate residues as analyzed by on-probe dephosphorylation. The current analysis contributes to our understanding of proteins expressed by the silk gland not only of the model lepidopteran B. mori, but also to proteins from other silk-producing insects such as Philosamia cynthia ricini.
| Original language | English |
|---|---|
| Pages (from-to) | 2586-2599 |
| Number of pages | 14 |
| Journal | Proteomics |
| Volume | 6 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Apr 1 2006 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
Cite this
Proteome analysis of silk gland proteins from the silkworm, Bombyx mori. / Zhang, Pingbo; Aso, Yoichi; Yamamoto, Kohji; Banno, Yutaka; Wang, Yongqiang; Tsuchida, Kozo; Kawaguchi, Yutaka; Fujii, Hiroshi.
In: Proteomics, Vol. 6, No. 8, 01.04.2006, p. 2586-2599.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Proteome analysis of silk gland proteins from the silkworm, Bombyx mori
AU - Zhang, Pingbo
AU - Aso, Yoichi
AU - Yamamoto, Kohji
AU - Banno, Yutaka
AU - Wang, Yongqiang
AU - Tsuchida, Kozo
AU - Kawaguchi, Yutaka
AU - Fujii, Hiroshi
PY - 2006/4/1
Y1 - 2006/4/1
N2 - The silk gland of Bombyx mori is an organ specialized for the synthesis and secretion of silk proteins. We report here the resolution of silk gland proteins by 2-DE and the identification of many of those proteins. This was accomplished by dissecting the glands into several sections, with each exhibiting more than 400 protein spots by 2-DE, of which 100 spots were excised and characterized by in-gel digestion followed by PMF. Ninety-three proteins were tentatively identified. These were then categorized into groups involved in silk protein secretion, transport, lipid metabolism, defense, etc. Western blotting of a 2-DE gel using an antibody of the carotenoid binding protein confirmed the presence of this protein in the silk gland. Proteins including fibroin L-chain and P25 were found as multiple isoforms, some of which contained differential amounts of phosphate residues as analyzed by on-probe dephosphorylation. The current analysis contributes to our understanding of proteins expressed by the silk gland not only of the model lepidopteran B. mori, but also to proteins from other silk-producing insects such as Philosamia cynthia ricini.
AB - The silk gland of Bombyx mori is an organ specialized for the synthesis and secretion of silk proteins. We report here the resolution of silk gland proteins by 2-DE and the identification of many of those proteins. This was accomplished by dissecting the glands into several sections, with each exhibiting more than 400 protein spots by 2-DE, of which 100 spots were excised and characterized by in-gel digestion followed by PMF. Ninety-three proteins were tentatively identified. These were then categorized into groups involved in silk protein secretion, transport, lipid metabolism, defense, etc. Western blotting of a 2-DE gel using an antibody of the carotenoid binding protein confirmed the presence of this protein in the silk gland. Proteins including fibroin L-chain and P25 were found as multiple isoforms, some of which contained differential amounts of phosphate residues as analyzed by on-probe dephosphorylation. The current analysis contributes to our understanding of proteins expressed by the silk gland not only of the model lepidopteran B. mori, but also to proteins from other silk-producing insects such as Philosamia cynthia ricini.
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UR - http://www.scopus.com/inward/citedby.url?scp=33646236906&partnerID=8YFLogxK
U2 - 10.1002/pmic.200500348
DO - 10.1002/pmic.200500348
M3 - Article
C2 - 16548058
AN - SCOPUS:33646236906
VL - 6
SP - 2586
EP - 2599
JO - Proteomics
JF - Proteomics
SN - 1615-9853
IS - 8
ER -