Purification of the delta isoenzyme of protein kinase C from the hepatopancreas of the shrimp Penaeus monodon with phosphorylation on tyrosine residues.
The delta isoenzyme of protein kinase C (PKC-delta), purified from the plasma membrane of the hepatopancreas of the shrimp Penaeus monodon is specifically phosphorylated at tyrosine residues, as demonstrated by specific dephosphorylation by phosphotyrosyl protein phosphatase from the hepatopancreas of the shrimp Penaeus monodon. The specific activity of purified PKC-delta was 200 units/mg of protein. The subunits of M(r) 66,000, 62,000, and 58,000 of PKC-delta were not autophosphorylated after the addition of phosphatidylserine and diolein. However, the purified PKC-delta was active and catalyzed the phosphorylation of myelin basic protein. The kinase activity of the purified PKC-delta could be decreased after treatment with phosphotyrosyl protein phosphatase.
Huang
C F
CF
Division of Biochemistry and Molecular Science, Academia Sinica, Nankang, Taipei, Taiwan.
Chuang
N N
NN
D000818:Animals; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D010179:Pancreas / Q000201:enzymology; D033561:Penaeidae / Q000201:enzymology*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000302:isolation & purification* / Q000378:metabolism; D051745:Protein Kinase C-delta; D014443:Tyrosine / Q000378:metabolism
D007527:Isoenzymes; D014443:Tyrosine; D011493:Protein Kinase C; D051745:Protein Kinase C-delta