Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1999-4-29
|
| pubmed:abstractText |
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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-924X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
125
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
64-9
|
| pubmed:dateRevised |
2007-12-19
|
| pubmed:meshHeading |
pubmed-meshheading:9880798-Agkistrodon,
pubmed-meshheading:9880798-Amino Acid Sequence,
pubmed-meshheading:9880798-Animals,
pubmed-meshheading:9880798-Crotalid Venoms,
pubmed-meshheading:9880798-Enzyme Stability,
pubmed-meshheading:9880798-Fibrinolytic Agents,
pubmed-meshheading:9880798-Metalloendopeptidases,
pubmed-meshheading:9880798-Molecular Sequence Data,
pubmed-meshheading:9880798-Sequence Homology, Amino Acid,
pubmed-meshheading:9880798-Substrate Specificity,
pubmed-meshheading:9880798-Viper Venoms
|
| pubmed:year |
1999
|
| pubmed:articleTitle |
Purification and amino acid sequence of brevilysin L6, a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom.
|
| pubmed:affiliation |
Department of Chemistry, Faculty of Science, Fukuoka University, Jonan-ku, Fukuoka, 814-0180, Japan.
|
| pubmed:publicationType |
Journal Article
|