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Molecular forms and subunit composition of a cyclic adenosine 3',5'-monophosphate-dependent protein kinase purified from bovine heart muscle.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Rubin, Charles S. Erlichman, Jack Rosen, Ora M. |
| Copyright Year | 1972 |
| Abstract | Abstract A cyclic adenosine 3',5'-monophosphate (cyclic AMP)-dependent protein kinase has been purified from bovine heart muscle. Its molecular weight was estimated to be 280,000 by gel filtration chromatography, and it was composed of cyclic AMP-independent protein kinase and cyclic AMP-binding subunits with molecular weights of 42,000 and 55,000, respectively. When the purified protein kinase was subjected to polyacrylamide gel electrophoresis, ultracentrifugation, or storage there appeared smaller forms of cyclic AMP-dependent kinase with molecular weights of approximately 140,000 and 90,000. A close structural relationship between all of these forms of protein kinase was suggested by the observation that each was composed of the same two kinds of subunits. |
| Starting Page | 36 |
| Ending Page | 44 |
| Page Count | 9 |
| File Format | PDF HTM / HTML |
| PubMed reference number | 4336043 |
| Journal | Medline |
| Volume Number | 247 |
| Issue Number | 1 |
| Alternate Webpage(s) | http://www.jbc.org/content/247/1/36.full.pdf |
| Journal | The Journal of biological chemistry |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
