Linked Life Data

12019457

Source:http://linkedlifedata.com/resource/pubmed/id/12019457

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-5-20
pubmed:abstractText
The gene of the basic phospholipase A(2) from Agkistrodon halys Pallas (BPLA(2) )was mutated site-directedly by polymerase chain reaction (PCR) and the residue Arg(34) of the encloding protein was substituted by Glu and Gln respectively. The mutant gene has been cloned into the expression vector pBLMVL2 and has been expressed in E.coli RR1 effectively. The protein was produced as insoluble inclusion bodies. After partial purification, the inclusion bodies were denatured and renatured into active form, and the renatured recombinant protein was purified by gel-filtration. The expression product has the same enzymatic activity as the denatured-refolded BPLA(2) and its hemolytic activity dropped distinctly, which suggest that the basic residue Arg(34) of BPLA(2) is a crucial amino acid residue during the process of hemolysis.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0582-9879
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
383-7
pubmed:dateRevised
2009-11-3
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
[The hemolytic site of the basic phospholipase A(2) from Agkistrodon halys pallas].
pubmed:affiliation
Institute of Biochemistry and Cell Biology, the Chinese Academy of Sciences, Shanghai 200031, China.
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't