Immunochemical characterization of the modulator protein of the ATP,Mg-dependent protein phosphatase.
Polyclonal antibodies raised against the modulator protein of the ATP,Mg-dependent protein phosphatase completely neutralize all known properties of the purified modulator: inhibition or inactivation of the phosphatase catalytic subunit as well as the kinase FA-mediated activation of the ATP,Mg-dependent phosphatase. They do not cross-react with phosphoinhibitor-1 or the phosphatase catalytic subunit. Direct analysis of boiled or unboiled skeletal muscle extracts by Western blotting reveals a 32 kDa polypeptide corresponding to the modulator protein as the most dominant protein staining band.
Vanden Abeele
C
C
Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Belgium.
Vandenheede
J R
JR
Merlevede
W
W
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D000906:Antibodies / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D007118:Immunoassay; D008274:Magnesium / Q000494:pharmacology*; D008970:Molecular Weight; D009124:Muscle Proteins; D009132:Muscles / Q000032:analysis*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors*; D010766:Phosphorylation; D011506:Proteins / Q000032:analysis* / Q000276:immunology / Q000494:pharmacology; D011817:Rabbits; D000097847:Protein Phosphatase Inhibitory Proteins
D000255:Adenosine Triphosphate; D000906:Antibodies; D008274:Magnesium; D009124:Muscle Proteins; D010749:Phosphoprotein Phosphatases; D011506:Proteins; C024833:protein phosphatase inhibitor-2; D000097847:Protein Phosphatase Inhibitory Proteins