Characterization of Bombyx mori Sericins by the Partial Amino Acid Sequences
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- Takasu Yoko
- National Institute of Agrobiological Sciences
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- Yamada Hiromi
- National Institute of Agrobiological Sciences Center for Ecological Research, Kyoto University
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- Saito Hitoshi
- National Institute of Agrobiological Sciences Present address: Department of Applied Biology, Kyoto Institute of Technology
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Abstract
To confirm the correspondence between sericin proteins and sericin genes of Bombyx mori, the partial amino acid sequences of cocoon sericins were determined by N-terminal sequencing of lysyl endopeptidase fragments and were then compared to the polypeptides derived from the Ser1 gene. It was determined that sericin M, which is the abundant component of sericin, was a product of the Ser1 gene, whereas sericin A, which distributes mainly in the floss and the outer layer of the cocoon, was not. In addition, sericin P was considered to be a smaller product of the Ser1 gene based on the cleavage pattern in the enzymatic digestion. It is expected that the properties of sericin A are different from those of sericins M and P because it does not have 38-amino acid repeats that constitute the major portion of the Ser1 proteins.<br>
Journal
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- Journal of Insect Biotechnology and Sericology
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Journal of Insect Biotechnology and Sericology 74 (3), 103-109, 2005
The Japanese Society of Sericultural Science
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Details 詳細情報について
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- CRID
- 1390282680172431744
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- NII Article ID
- 130004464099
- 10016770298
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- NII Book ID
- AA11558849
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- ISSN
- 18847978
- 13468073
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- NDL BIB ID
- 7692590
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- CiNii Articles
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- Abstract License Flag
- Disallowed