Affordable Access

Purification and properties of protein kinase C from bovine polymorphonuclear leucocytes.

Authors
Type
Published Article
Journal
Biochimica et Biophysica Acta
0006-3002
Publisher
Elsevier
Publication Date
Volume
885
Issue
2
Pages
170–175
Identifiers
PMID: 3947678
Source
Medline

Abstract

A calcium-activated, phospholipid-dependent protein kinase (protein kinase C) was purified to near homogeneity from bovine polymorphonuclear leucocytes. The purified enzyme had a specific activity of 10 000 U/mg protein and on SDS gelelectrophoresis the Mr was 88 000. The enzyme activity was almost totally dependent upon phosphatidylserine and could be strongly activated by Ca2+ concentrations in the micromolar range. At lower concentrations of calcium (less than 1 X 10(-7) M) the enzyme was only activated by the simultaneous presence of phosphatidylserine and diolein. Phorbol 12-myristate 13-acetate mimicked the effect of diolein and partially activated the enzyme. Protein kinase C activity and the phorbolester binding protein co-purified throughout all the purification steps.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments