Catalytic Subunit of Cyclic AMP-Dependent Protein Kinase

1999 ◽  
Vol 82 (2-3) ◽  
pp. 133-141 ◽  
Author(s):  
Susan S Taylor ◽  
Elzbieta Radzio-Andzelm ◽  
Madhusudan ◽  
Xiaodong Cheng ◽  
Lynn Ten Eyck ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Catalytic Subunit ◽  
Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals A relative of the catalytic subunit of cyclic AMP-dependent protein kinase in Aplysia spermatozoa.

1990 ◽  
Vol 10 (12) ◽  
pp. 6775-6780 ◽  
Author(s):  
S Beushausen ◽  
H Bayley
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Cyclic Nucleotide ◽  
Aplysia Californica ◽  
Catalytic Subunit ◽  
Spermatogenic Cells ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Mature Spermatozoa ◽  
Kinase Subfamily

Transcripts encoding CAPL-B, an apparent member of the cyclic-nucleotide-regulated kinase subfamily in Aplysia californica, are found exclusively in the ovotestis and are concentrated in meiotic and postmeiotic spermatogenic cells. The CAPL-B polypeptide is present in mature spermatozoa, suggesting that the kinase plays a part in regulating events associated with fertilization.

scholarly journals The inhibitor protein of the cyclic AMP-dependent protein kinase-catalytic subunit interaction. Composition of multiple complexes

1988 ◽  
Vol 256 (3) ◽  
pp. 785-789 ◽  
Author(s):  
S M Van Patten ◽  
A Hotz ◽  
V Kinzel ◽  
D A Walsh
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Catalytic Subunit ◽  
Inhibitor Protein ◽  
Multiple Forms ◽  
Subunit Interaction ◽  
Dependent Protein Kinase ◽  
Bovine Heart ◽  
Dependent Protein ◽  
Multiple Species

It has been previously demonstrated that the combination of pure preparations of the inhibitor protein of the cyclic AMP-dependent protein kinase and the catalytic subunit of this enzyme resulted in the formation of multiple complexes [Van Patten, Fletcher & Walsh (1986) J. Biol. Chem. 261, 5514-5523]. In the present study it is demonstrated that these multiple species occur because the bovine heart protein kinase preparation contains multiple forms of catalytic subunit [Kinzel, Hotz, König, Gagelmann, Pyerin, Reed, Köbler, Hofmann, Obst, Gensheimer, Goldblatt & Shaltiel (1987) Arch. Biochem. Biophys. 253, 341-349].

scholarly journals Antiserum against the catalytic subunit of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase. Reactivity towards various protein kinases

1980 ◽  
Vol 192 (1) ◽  
pp. 223-230 ◽  
Author(s):  
G Schwoch ◽  
A Hamann ◽  
H Hilz
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Rat Liver ◽  
Catalytic Subunit ◽  
Type Ii ◽  
Dependent Protein Kinase ◽  
Subunit C ◽  
Bovine Heart ◽  
Dependent Protein

An antiserum against the catalytic subunit C of cyclic AMP-dependent protein kinase, isolated from bovine heart type II protein kinase, was produced in rabbits. Reaction of the catalytic subunit with antiserum and separation of the immunoglobulin G fraction by Protein A-Sepharose quantitatively removed the enzyme from solutions. Comparative immunotitration of protein kinases showed that the amount of antiserum required to eliminate 50% of the enzymic activity was identical for pure catalytic subunit, and for holoenzymes type I and type II. The reactivity of the holoenzymes with the antiserum was identical in the absence or the presence of dissociating concentrations of cyclic AMP. Most of the holoenzyme (type II) remains intact when bound to the antibodies as shown by quantification of the regulatory subunit in the supernatant of the immunoprecipitate. Titration with the antibodies also revealed the presence of a cyclic AMP-independent histone kinase in bovine heart protein kinase I preparations obtained by DEAE-cellulose chromatography. Cyclic AMP-dependent protein kinase purified from the particulate fraction of bovine heart reacted with the antiserum to the same degree as the soluble enzyme, whereas two cyclic AMP-independent kinases separated from the particle fraction neither reacted with the antiserum nor influenced the reaction of the antibodies with the cyclic AMP-dependent protein kinase. Immunotitration of the protein kinase catalytic subunit C from rat liver revealed that the antibodies had rather similar reactivities towards the rat liver and the bovine heart enzyme. This points to a relatively high degree of homology of the catalytic subunit in mammalian tissues and species. Broad applicability of the antiserum to problems related to cyclic AMP-dependent protein kinases is thus indicated.

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