Linked Life Data

1282356

Source:http://linkedlifedata.com/resource/pubmed/id/1282356

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-2-11
pubmed:abstractText
In order to covalently bind the hydrolyzed thiol ester groups of the human alpha 2-macroglobulin (alpha 2M) transformed by methylamine, the phospholipase A2 (PLA2), a small enzyme (M(r) = 13,000) from Naja nigricollis snake venom was activated by succinimidyl 4-(maleimidomethyl)cyclohexane-1-carboxylate (SMCC). Average images determined from electron micrographs of the methylamine-transformed alpha 2M, with and without activated PLA2, were determined by image processing and compared. A localization of the PLA2 was achieved by subtracting the average image of alpha 2M transformed by methylamine from that containing PLA2. The results are consistent with previous work showing the central localization of chymotrypsin trapped in alpha 2M. They also suggest that the four thiol esters are located near the center of the alpha 2M molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1047-8477
pubmed:author
pubmed:issnType
Print
pubmed:volume
108
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
Electron microscopy of alpha 2-macroglobulin with a thiol ester bound ligand.
pubmed:affiliation
Laboratoire de Biochimie Fondamentale, Université François Rabelais, CNRS URA 1334, Tours, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't