In:
FEBS Letters, Wiley, Vol. 265, No. 1-2 ( 1990-06-04), p. 117-120
Abstract:
A [ 3 H]azidophenacyl ester of PGE 2 ([ 3 H]azido‐PGE 2 ) was synthesized and used to photoaffinity label the protein component of the high affinity PGE 2 binding site in cardiac sarcolemma membrane. Photolysis of the isolated cardiac sarcolemmal vesicles in the presence of [ 3 H]azido‐PGE 2 resulted in the covalent labelling of a protein component that migrated on sodium dodecyl sulfate‐polyacrylamide gels with an apparent molecular weight of 100 000. Incorporation of the [ 3 H]azido‐PGE 2 did not occur in the absence of photolysis. The photolabelling of the 100‐kDa protein by [ 3 H]azido‐PGE 2 was inhibited by excess unlabelled PGE 2 and arido‐PGE 2 . Specific binding of [ 3 H]azido‐PGE 2 was displaced by excess unlabelled PGE 2 or azido‐PGE 2 , but not PGF 2α , 6‐keto‐PGF 1α or PGD 2 . These results indicate that the 100‐kDa photoaffinity labelled [ 3 H]azido‐PGE 2 binding protein contains the binding site for PGE 2 in isolated cardiac sarcolemma membranes.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(90)80898-S
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
1460391-3
SSG:
12