Compartmentalization of Cyclic AMP-Dependent Protein Kinases in Human Erythrocytes

The human erythrocyte contains two types of cyclic AMP-dependent protein kinase. The membrane-associated protein kinase holoenzyme can be released intact by hypotonic treatment at alkaline pH. Chromatography on DEAE-cellulose and molecular weight determinations demonstrate that this enzyme is a type...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1978-12, Vol.75 (12), p.5926-5930
Main Authors: Dreyfuss, Gideon, Schwartz, Kenneth J., Blout, Elkan R.
Format: Article
Language:English
Subjects:
Biochemistry
Cell Compartmentation
Chromatography
Cyclic AMP - metabolism
Cytoplasm
Cytoplasm - enzymology
Detergents
Enzymes
Erythrocyte membrane
Erythrocyte Membrane - enzymology
Erythrocytes
Erythrocytes - metabolism
Gels
Humans
Kinetics
Macromolecular Substances
Membrane proteins
Molecular Weight
Polyethylene Glycols
Protamines
Protein Kinases - blood
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Description
Summary:The human erythrocyte contains two types of cyclic AMP-dependent protein kinase. The membrane-associated protein kinase holoenzyme can be released intact by hypotonic treatment at alkaline pH. Chromatography on DEAE-cellulose and molecular weight determinations demonstrate that this enzyme is a type I cyclic AMP-dependent protein kinase, while the predominant cyclic AMP-dependent protein kinase found in the cytoplasm is type II. The catalytic subunits of the two types of kinase found in the erythrocyte are identical, but the regulatory subunits, which distinguish the two types of kinase, determine their localization within the cell. It is proposed that the regulatory subunit of the type I enzyme, in addition to binding the catalytic subunit, interacts specifically with one or more membrane proteins and that this interaction may serve to position the kinase in preferential proximity to protein substrates.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.75.12.5926