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Isolation of homologous and heterologous complexes between catalytic and regulatory components of adenylate cyclase by forskolin—Speharose
Author(s) -
Pfeuffer Thomas,
Gaugler Bernhard,
Metzger Heinz
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80040-4
Subject(s) - heterologous , adenylate kinase , cyclase , forskolin , gtp' , chemistry , biochemistry , heterologous expression , sepharose , microbiology and biotechnology , biology , enzyme , receptor , recombinant dna , gene
Homologous and heterologous complexes between catalytic and GTP‐binding components can be isolated by means of immobilized succinyldeacetylforskolin (forskolin—Sepharose). A heterologous complex is formed by reconstitution of forskolin—Sepharose bound catalytic function from rabbit myocardial membranes with the homogeneous [ 3 H]methyl‐GTP‐binding protein from duck erythrocyte membranes. Analysis of the reconstituted complex by sodium dodecyl sulfate polyacrylamide gelelectrophoresis reveals that only the M r 42 000 component of the GTP‐binding protein's M r 42 000/ M r 35 000 heterodimer contributes to the formation of active adenylate cyclase.