Pub. Date : 1987 Jul 14
PMID : 3663598
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | A calmodulin-sensitive adenylate cyclase has been purified to apparent homogeneity from bovine cerebral cortex using calmodulin-Sepharose followed by forskolin-Sepharose and wheat germ agglutinin-Sepharose. | Sepharose | CaM5 | Triticum aestivum |
2 | A calmodulin-sensitive adenylate cyclase has been purified to apparent homogeneity from bovine cerebral cortex using calmodulin-Sepharose followed by forskolin-Sepharose and wheat germ agglutinin-Sepharose. | Colforsin | CaM5 | Triticum aestivum |
3 | A calmodulin-sensitive adenylate cyclase has been purified to apparent homogeneity from bovine cerebral cortex using calmodulin-Sepharose followed by forskolin-Sepharose and wheat germ agglutinin-Sepharose. | Sepharose | CaM5 | Triticum aestivum |
4 | A calmodulin-sensitive adenylate cyclase has been purified to apparent homogeneity from bovine cerebral cortex using calmodulin-Sepharose followed by forskolin-Sepharose and wheat germ agglutinin-Sepharose. | Sepharose | CaM5 | Triticum aestivum |
5 | This polypeptide was a major component of the protein purified through calmodulin-Sepharose. | Sepharose | CaM5 | Triticum aestivum |
6 | The catalytic subunit was stimulated 3-4-fold by calmodulin (CaM) with a turnover number greater than 1000 min-1 and was directly inhibited by adenosine. | Adenosine | CaM5 | Triticum aestivum |
7 | The catalytic subunit was stimulated 3-4-fold by calmodulin (CaM) with a turnover number greater than 1000 min-1 and was directly inhibited by adenosine. | Adenosine | CaM5 | Triticum aestivum |
8 | The catalytic subunit of the enzyme interacted directly with 125I-CaM on a sodium dodecyl sulfate-polyacrylamide gel overlay system, and this interaction was Ca2+ concentration dependent. | Sodium Dodecyl Sulfate | CaM5 | Triticum aestivum |
9 | The catalytic subunit of the enzyme interacted directly with 125I-CaM on a sodium dodecyl sulfate-polyacrylamide gel overlay system, and this interaction was Ca2+ concentration dependent. | polyacrylamide | CaM5 | Triticum aestivum |
10 | These data illustrate that the catalytic subunit of the calmodulin-sensitive adenylate cyclase is a glycoprotein which interacts directly with calmodulin and that adenosine can inhibit the enzyme without intervening receptors or G coupling proteins. | Adenosine | CaM5 | Triticum aestivum |