Properties of the regulatory subunit of cAMP-dependent protein kinase type II from human brain

Biochem Mol Biol Int. 1996 Dec;40(6):1159-66. doi: 10.1080/15216549600201793.

Abstract

The regulatory subunit type II (RII) of cAMP-dependent protein kinase purified from human brain was represented by two proteins with apparent molecular masses of 51-52 kD and 54 kD. Dephosphorylation of human RII containing 3 mol phosphate/mol protein did not change the electrophoretic pattern. One-dimensional peptide mapping of 51-52 kD and 54 kD proteins after digestion with St. aureus V8 protease evidenced to their being distinct proteins. The data obtained permit to assume that human RII of neural type is represented by two isoforms.

MeSH terms

  • Animals
  • Brain / enzymology*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism
  • Cattle
  • Cyclic AMP / metabolism
  • Cyclic AMP-Dependent Protein Kinase Type II
  • Cyclic AMP-Dependent Protein Kinases / chemistry*
  • Cyclic AMP-Dependent Protein Kinases / isolation & purification
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Immunoblotting
  • Intracellular Signaling Peptides and Proteins*
  • Isoenzymes / chemistry
  • Molecular Weight
  • Peptide Mapping
  • Phosphates / analysis
  • Phosphorylation
  • Swine

Substances

  • Carrier Proteins
  • Intracellular Signaling Peptides and Proteins
  • Isoenzymes
  • Phosphates
  • protein kinase modulator
  • Cyclic AMP
  • Cyclic AMP-Dependent Protein Kinase Type II
  • Cyclic AMP-Dependent Protein Kinases