Purification of bovine brain adenylyl cyclase with a novel derivative of forskolin: evidence for a high specific activity form of the enzyme
| Autor: | J D Robbins, Malcolm Moos, Appel L, Morris Di, Seamon Kb |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
ADCY6
Forskolin ADCY5 Time Factors Molecular Structure ADCY9 Colforsin Osmolar Concentration Brain Reproducibility of Results General Medicine ADCY3 Biochemistry ADCY10 Adenylyl cyclase chemistry.chemical_compound chemistry Animals Specific activity Cattle Adsorption Diterpenes Biotechnology Adenylyl Cyclases |
| Zdroj: | Preparative biochemistrybiotechnology. 26(2) |
| ISSN: | 1082-6068 |
| Popis: | An improved affinity support for the purification of adenylyl cyclase was prepared from 7-desacetyl-7-aminoethylaminocarbonyl forskolin. This analog allows convenient synthesis of an affinity matrix that is chemically stable, withstanding repeated use for up to two years, and efficient, yielding purifications of adenylyl cyclase from solubilized bovine brain membranes of 2,000–6,000 fold in a single step. Immunoblotting data suggest that the majority of the enzyme purified in this fashion differs from forms described previously. Since the specific activity of this preparation is substantially higher than that described in previous reports, it is possible that the purification described here selects, presumably on the basis of affinity for forskolin, for a form of adenylyl cyclase with higher specific activity than any described previously. |
| Databáze: | OpenAIRE |
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