Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-5-23
pubmed:abstractText
Hemolysin is one of the most hazardous components in the venom of Cyanea nozakii Kishinouye. Here we describe the purification and in vitro characterization of the hemolysin, which we named CnPH. The CnPH was isolated by anion-exchange and size-exclusion chromatography from the nematocyst venom. Two protein bands with molecular masses of 20 kDa, 60 kDa respectively were shown in the reducing SDS-PAGE analysis of the CnPH. And Approximately 5 ?g/mL of the CnPH resulted in 50% hemolysis of the erythrocyte suspension. The hemolytic activity of the CnPH was both temperature and pH dependent. Moreover, it was significantly inhibited in the presence of divalent metal cations, including Cu(2+), Mg(2+), Mn(2+), Zn(2+) and Ca(2+), but enhanced in the presence of EDTA. However, how CnPH performs its hemolytic activity is not yet clear, therefore the mechanism of the hemolytic activity of the CnPH is under research.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1879-0003
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14-9
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Two-step purification and in vitro characterization of a hemolysin from the venom of jellyfish Cyanea nozakii Kishinouye.
pubmed:affiliation
Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, Qingdao 266071, China. lirongfeng07@qdio.ac.cn
pubmed:publicationType
Journal Article