z-logo
open-access-imgOpen Access
Calf‐Ovary Protein Kinases Dependent on Adenosine 3′: 5′‐Monophosphate
Author(s) -
SALOKANGAS Anneli,
TALMADGE Kenneth,
BECHTEL Elke,
EPPENBERGER Urs,
CHRAMBACH Andreas
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11331.x
Subject(s) - polyacrylamide gel electrophoresis , kinase , isoelectric focusing , cytosol , biochemistry , gel electrophoresis , adenosine , biology , protein kinase a , enzyme , microbiology and biotechnology , chemistry
High resolving power and quantitative application of polyacrylamide‐gel electrophoresis at various pore sizes and electrofocusing provide resolution of a calf‐ovarian protein‐kinase system at an increased level of magnification, as well as optimal preparative routes. Three protein kinases dependent on adenosine 3′:5′‐monophosphate are distinguished by polyacrylamide gel electrophoresis in calf ovarian cytosol. These enzymes which are observed in the pH range 7.5–10.2, appear to be aggregates of a common subunit or monomer. The three kinases are, by the criteria of polyacrylamide gel electrophoresis, distinct from three adenosine‐3′:5′‐monophosphate‐binding proteins found in the calf ovarian system. Analysis by electrofocusing on polyacrylamide gel shows that conventionally purified preparations of the major kinase of cytosol contain an overwhelming majority of contaminant proteins.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here