Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1982-6-24
pubmed:abstractText
A photoaffinity derivative of salmon calcitonin has been produced by transglutaminase-mediated incorporation of N-(beta-aminoethyl)-4-azido-2-nitroaniline into the hormone. The derivative, purified by high pressure liquid chromatography, retained the abilities to bind to cultured T47D breast cancer cells and to stimulate adenylate cyclase in these cells. In both these respects it was equipotent with synthetic salmon calcitonin. Photolysis of the 125I-labeled photoactive salmon calcitonin derivative bound to T47D cells was accompanied by specific labeling of only one component (Mr approximately 85,000) as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Labeling was observed only upon photolysis and was inhibited by unlabeled synthetic salmon calcitonin but not by the inactive calcitonin analogue, 8-glycine human calcitonin. Reduction did not alter the apparent molecular weight of the calcitonin receptor complex. No macromolecular forms of calcitonin were produced by photolysis in the absence of T47D cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5846-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Covalent cross-linking of a photoactive derivative of calcitonin to human breast cancer cell receptors.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't