Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins.

Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Research Abstract Details 

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Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Abstract Text:

H Takagi,H Narumi,K Nakamura,T Sasaki,

A cDNA clone of silkworm (Bombyx mori) larval hemolymph antitrypsin (sw-AT) has been isolated from a fat body cDNA library. The cDNA has an open reading frame which codes a 392-amino acid residue polypeptide comprising a 16-residue signal peptide and a 376-residue mature sw-AT of Mr 41,805. The reactive site of sw-AT for inhibition of bovine trypsin [Sasaki, T. et al. (1987) J. Biochem. 102, 433-441] was identified as Lys343-Val344. Alignment of the sw-AT amino acid sequence with those of 11 members of the serpin superfamily of proteins clearly confirmed the homology of sw-AT with serpins. The amino acid sequence of sw-AT is 56% identical with that of the proteinase inhibitor from a lepidopteron, Manduca sexta [Kanost, M.R. et al. (1989) J. Biol. Chem. 264, 965-972], but the sequence around the reactive site shows no homology and the inhibitory specificity for proteinases is very different.

Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Publishing Authors By Initials

H Takagi,H Narumi,K Nakamura,T Sasaki,

For similar chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: protease inhibitors: serine proteinase inhibitors: trypsin inhibitors research abstracts see: chemical actions and uses: pharmacologic actions: molecular mechanisms of pharmacological action: enzyme inhibitors: protease inhibitors: serine proteinase inhibitors: trypsin inhibitors research

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Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 108

Page Numbers: 372-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1990

Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Keywords Mesh Terms:

KEYWORDS: Trypsin Inhibitors

MESH TERMS: genetics

Chemical & Substance for Abstract: Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins. Information

Substance Name: DNA

Registry Number: 9007-49-2

Grant and Affiliation Information for Amino acid sequence of silkworm (Bombyx mori) hemolymph antitrypsin deduced from its cDNA nucleotide sequence: confirmation of its homology with serpins.

AFFILIATION: Department of Food Science, School of Agriculture, Nagoya University, Aichi.

Country: JAPAN

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MEDLINETA: J Biochem

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