Linked Life Data

7060561

Source:http://linkedlifedata.com/resource/pubmed/id/7060561

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-5-21
pubmed:abstractText
Upon tryptic activation of pure human prophospholipase A2, a heptapeptide is released from the N-terminal part of the protein yielding active phospholipase A2 (EC 3.1.1.4). Both the kinetics of the activation process and the amino acid sequence of the activation peptide strongly resemble those of pancreatic zymogens of other mammalian sources. The kinetic properties of human phospholipase A2 and its zymogen are compared with those of the corresponding porcine enzyme using substrates present at micelles, molecular dispersed solutions or as monomolecular surface films. The most obvious difference between the human and porcine phospholipase A2 is the low enzyme activity of the former protein at pH 8.0 as compared to pH 6.0, both against micellar and monomeric substrates. Neither the Ca2+ binding properties nor the inhibition of the human enzyme using haloketones can easily explain this different pH optimum. The sequence analysis of the N-terminal region of the first 40 residues is reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region.
pubmed:publicationType
Journal Article, Comparative Study