Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus.

Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Research Abstract Details 

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Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Abstract Text:

S Fujimura,K Oshikawa,S Terada,E Kimoto,

The complete amino acid sequence of brevilysin H6 (H6), a zinc-protease isolated from Gloydius halys brevicaudus venom, was determined by a manual Edman degradation method. H6 has an amino-terminal pyroglutamic acid and consists of a total of 419 residues. An N-linked sugar chain is attached at Asn-181. The molecule is composed of three domains (metalloprotease, disintegrin-like and cysteine-rich domains), as commonly found in other high molecular mass metalloproteases from snake venoms. In the absence of calcium ions, H6 is autocatalytically degraded with a half-life of 47 min to give 29 and 45 kDa fragments, which correspond to residues 208-419 and 99-419 of H6, respectively. Thus, the autoproteolysis seemed to start from the cleavage of either the Leu(98)-Leu(99) or Asp(207)-Ile(208) bond. Calcium ions suppressed both the formation of the 45 kDa fragment and the rate of autoproteolysis. Calcium ions also contributed to the stability of H6 against pH, heating, urea and cysteine. More than twenty-five peptide bonds adjacent to hydrophobic residues in the metalloprotease domain were progressively cleaved during the autoproteolysis.

Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Publishing Authors By Initials

S Fujimura,K Oshikawa,S Terada,E Kimoto,

For similar snake venoms: viper venoms research abstracts see: snake venoms: viper venoms research

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Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 128

Page Numbers: 167-73

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 2000

Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Keywords Mesh Terms:

KEYWORDS: Viper Venoms

MESH TERMS: chemistry

Chemical & Substance for Abstract: Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus. Information

Substance Name: brevilysin L6

Registry Number: EC 3.4.24.-

Grant and Affiliation Information for Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus.

AFFILIATION: Department of Chemistry, Faculty of Science, Fukuoka University, Nanakuma, Jonan-ku, Fukuoka 814-0180, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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