Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin.

Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Research Abstract Details 

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Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Abstract Text:

K Tsujimoto,H Takagi,M Takahashi,H Yamada,S Nakamori,

The silk proteins, fibroin and sericin, are produced in the silk gland of Bombyx mori, and hydrophilic sericin envelops fibroin with successive sticky layers in the formation of a cocoon. To study the biological functions of sericin, we focused on the serine-rich sericin peptide consisting of 38 amino acids, which is a highly conserved and internally repetitive sequence of a sericin protein. The corresponding gene was chemically synthesized, and the PCR-amplified gene was ligated to oligomerize sericin peptide and fused at the amino terminus to a His-tagged and proteolytic cleavage sequence in an inducible expression vector. When the dimers of sericin peptides were overexpressed in Escherichia coli, the transformants showed a prominent increase in cell viability after freezing in medium. Further, the purified dimeric sericin peptide from E. coli was found to be effective in protecting lactate dehydrogenase from denaturation caused by freeze-thaw. Both of these protective effects against freezing stress in cells and proteins were also observed with sericin hydrolysate. These results indicate that this unique sericin peptide, like sericin, has a high cryoprotective activity and will be valuable as a new biomaterial for industrial use.

Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Publishing Authors By Initials

K Tsujimoto,H Takagi,M Takahashi,H Yamada,S Nakamori,

For similar investigative techniques: genetic techniques: gene transfer techniques: transfection: transformation, bacterial research abstracts see: investigative techniques: genetic techniques: gene transfer techniques: transfection: transformation, bacterial research

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Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 129

Page Numbers: 979-86

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 2001

Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Keywords Mesh Terms:

KEYWORDS: Transformation, Bacterial

MESH TERMS: metabolism

Chemical & Substance for Abstract: Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin. Information

Substance Name: L-Lactate Dehydrogenase

Registry Number: EC 1.1.1.27

Grant and Affiliation Information for Cryoprotective effect of the serine-rich repetitive sequence in silk protein sericin.

AFFILIATION: Technology Department, Seiren Co. Ltd., Keya, Fukui 918-8560, Japan.

Country: Japan

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MEDLINETA: J Biochem

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