Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom.

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Abstract Text:

S Terada,J Hori,S Fujimura,E Kimoto,

A non-hemorrhagic proteinase, brevilysin L6 (L6), has been purified to homogeneity from Agkistrodon halys brevicaudus venom by gel filtration and DEAE-Toyopearl 650M chromatography. It is an acidic protein with an isoelectric point of 4.8, and its molecular mass was estimated to be 21.5 kDa by SDS-PAGE. The optimum pH of L6 was about 9. EDTA and o-phenanthroline inhibited the proteolytic activity, suggesting that L6 is a metalloprotease. Cysteine also inhibited the activity of L6, but glutathione did not. The protein was stable in the pH range of 5-8.5 and below 40 degreesC. Calcium ions had no effect on the proteolytic activity of L6 or on its thermal stability. The enzyme preferentially cleaved X-Leu, X-Phe, X-Val, and X-His bonds. L6 showed weak alpha-fibrinogenase activity. The complete amino acid sequence of L6 was also determined by manual Edman degradation. L6 is a non-glycosylated single-chain polypeptide consisting of 203 residues with an N-terminal pyroglutamic acid and a calculated molecular weight of 22,713 Da. Its entire sequence is highly homologous to those of other metalloproteases from various snake venoms. A zinc-binding motif, HEXXHXXGXXH, is located at residues 143-153 in the sequence of L6.

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Publishing Authors By Initials

S Terada,J Hori,S Fujimura,E Kimoto,

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

PUBMED ID PMID:

MEDLINE DATE:

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 125

Page Numbers: 64-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 1999

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Keywords Mesh Terms:

KEYWORDS: Viper Venoms

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom. Information

Substance Name: brevilysin L6

Registry Number: EC 3.4.24.-

Grant and Affiliation Information for Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom.

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

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom Related Publications

• A study on the reaction of human erythrocytes with hydrogen peroxide.
• Amino acid sequences of Kunitz family subtilisin inhibitors from seeds of Canavalia lineata.
• Effects of anion transport inhibitors on hemolysis of human erythrocytes under hydrostatic pressure.
• Effects of cross-linking of membrane proteins on vesiculation induced by dimyristoylphosphatidylcholine in human erythrocytes.
• Effects of drugs, salts, and phospholipid vesicles on hemoglobin release from hydrostatic pressure-treated human erythrocytes.
• Effects of pH on membrane fluidity of human erythrocytes.
• Effects of temperature and cholesterol on human erythrocyte membranes.
• Hemolytic properties of Ca(2+)-treated human erythrocytes under hydrostatic pressure.
• Hemolytic properties under hydrostatic pressure of neuraminidase- or protease-treated human erythrocytes.
• Manipulation for Plasmid Elimination by Transforming Synthetic Competitors Diversifies Lactococcus lactis Starters Applicable to Food Products.
• Nicotianamine preferentially inhibits Angiotensin I-converting enzyme.
• Preparation of recombinant murine tumor necrosis factor-alpha in Escherichia coli: a rapid method to remove tags from fusion proteins by thrombin-cleavage and ion-exchange chromatography.
• Primary structure and autoproteolysis of brevilysin H6 from the venom of Gloydius halys brevicaudus.
• Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom.
• Purification and characterization of two Kunitz family subtilisin inhibitors from seeds of Canavalia lineata.
• Release of spectrin-containing vesicles from human erythrocyte ghosts by dimyristoylphosphatidylcholine.
• Vesiculation induced by hydrostatic pressure in human erythrocytes.
• [Experimental study of the aortic annulus enlargement (author's transl)]
• [Historical review of surgery of the heart and great vessels in Japan (author's transl)]
• [Long-term follow up of sphincterotomy in spinal cord injured men]
• [Pleural effusion due to rupture of benign cystic teratoma into left pleural cavity: a review of the Japanese literature]