Linked Life Data

7597722

Source:http://linkedlifedata.com/resource/pubmed/id/7597722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-8-3
pubmed:abstractText
Chemical modification studies have been carried out on the sea anemone polypeptide anthopleurin-A in order to clarify the role of Arg-14 in its cardiac stimulatory activity. Reaction with 1,2-cyclohexanedione at 37 degrees C produced a range of protein products, including some with amino group modifications. These side-reactions were eliminated by prior citraconylation of the amino groups, which, following reaction with cyclohexanedione, could be reversed under conditions which preserved the cyclohexanedione adduct. Citraconylation of the three amino groups, one from the N-terminus and two from Lys-37 and Lys-48, destroyed the cardiac stimulatory activity of the molecule, but this was fully recoverable upon reversal of this reaction. It appears that one or more of the amino groups is essential for activity. Anthopleurin-A contains only one arginine residue, and this was confirmed as the site of modification by cyclohexanedione by showing that the product was refractory to proteolysis by trypsin, which normally cleaves the molecule at this residue. The positive inotropic activity of the cyclohexanedione adduct on isolated guinea-pig atria was identical to that of unmodified anthopleurin-A, indicating that the side-chain of Arg-14 is not required for cardiotonic activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
187-99
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Chemical modification of cationic groups in the polypeptide cardiac stimulant anthopleurin-A.
pubmed:affiliation
School of Biochemistry, University of New South Wales, Kensington, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't