PMID: 8939354Oct 1, 1996Paper

Calmodulin-dependent protein kinase II from bovine cardiac muscle: purification and differential activation by calcium

Cell Calcium
R KakkarR K Sharma

Abstract

Calmodulin-dependent protein kinase II was purified to apparent homogeneity with a high yield from the total calmodulin-binding protein fraction of bovine cardiac muscle in a single step by gel filtration column chromatography. This procedure is simple and suitable for adaptation to large scale preparations. The purified calmodulin-dependent protein kinase has a specific enzymic activity of 2.4 mumol/min/mg when mixed histone was used as a substrate. The preparation of enzyme appears to be homogeneous when examined by SDS-PAGE. The molecular weight of the enzyme was determined to be 570 kDa by gel filtration. SDS-PAGE of the enzyme subunit showed a single protein band with an apparent molecular weight of 56 kDa. These results suggest that the calmodulin-dependent protein kinase II from bovine heart is composed of 10 identical subunits. Anti-peptide antibody raised against multifunctional calmodulin-dependent protein kinase II from rat brain showed a single immunoreactive band of 56 kDa on Western blot. These results suggested that bovine cardiac muscle calmodulin-dependent protein kinase could resemble the brain isozyme. Calmodulin-dependent protein kinase II undergoes autophosphorylation with a maximal incorporation of 1 mol o...Continue Reading

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Jan 1, 1992·Annual Review of Biochemistry·P I Hanson, H Schulman
Jul 31, 1992·Biochemical and Biophysical Research Communications·J A BarnesR K Sharma
May 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·D C BarteltR L Hammell
May 31, 1985·Biochemical and Biophysical Research Communications·T Yamauchi, H Fujisawa
Jun 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·Y LaiP Greengard
Feb 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·C Y HuangR K Sharma
Jan 1, 1982·Advances in Protein Chemistry·C B Klee, T C Vanaman
Aug 5, 1980·Biochemistry·T H Crouch, C B Klee
Jan 27, 1995·Cell·D E Clapham
Mar 15, 1993·Biochemical and Biophysical Research Communications·G Y ZhangR K Sharma
Jan 1, 1993·Neurochemical Research·H Schulman, P I Hanson

❮ Previous
Next ❯

Citations

Jun 21, 2005·Proceedings of the National Academy of Sciences of the United States of America·Jin O-UchiSatoshi Kurihara

❮ Previous
Next ❯

Related Concepts

Related Feeds

Antibody Specificity

Antibodies produced by B cells are highly specific for antigen as a result of random gene recombination and somatic hypermutation and affinity maturation. As the main effector of the humoral immune system, antibodies can neutralize foreign cells. Find the latest research on antibody specificity here.