| Autor: |
J. Antonio Villamarín, Montserrat Recalde Fernández, J.Ignacio Ramos Martı́nez, M.Dolores Vázquez-Illanes, Jesús Cao |
| Rok vydání: |
1995 |
| Předmět: |
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| Zdroj: |
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 111:453-462 |
| ISSN: |
1096-4959 |
| DOI: |
10.1016/0305-0491(95)00016-2 |
| Popis: |
The catalytic subunit of cyclic AMP-dependent protein kinase was isolated from mantle tissue of the sea mussel Mytilus galloprovincialis and purified to apparent homogeneity using a simple two-step procedure. The purified enzyme had a molecular weight of 40 ± 1.5 kDa on electrophoresis under denaturing conditions, Stokes' radius 25.8 A and isoelectric point (pI) 8.5. Kinetic experiments showed that the mussel enzyme used Mg 2+ as preferred divalent cation (it was inactive in the presence of Mn 2+ and the apparent K m values for MgATP and histone II-A were 43 ± 7 μM and 1.72 ± 0.65 mg/ml, respectively. Mussel C-subunit was inhibited by the regulatory subunit (type RII) of cAMP-dependent protein kinase from mammals and also by the inhibitor peptide PKI(5–24) with a I 50 of 6.5 ± 1.6 nM. When RII-subunit from porcine heart was incubated, in the presence of [ γ - 32 P]ATP, with C-subunit from mussel or porcine, a comparable rate of regulatory subunit phosphorylation was achieved. These physical and biochemical properties lead to the conclusion that the catalytic subunit of cAMP-dependent protein kinase from a bivalve mollusc is closely related to its counterparts from mammalian sources. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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