Caldesmon: anomalous electrophoretic behaviour in polyacrylamide gel

P Cavanni; P Cavallini; E Ratti; G Gaviraghi; L Dalla Libera

doi:10.1016/0006-291x(89)91637-9

Caldesmon: anomalous electrophoretic behaviour in polyacrylamide gel

Biochem Biophys Res Commun. 1989 Apr 14;160(1):174-80. doi: 10.1016/0006-291x(89)91637-9.

Authors

P Cavanni¹, P Cavallini, E Ratti, G Gaviraghi, L Dalla Libera

Affiliation

¹ Institute of General Pathology, University of Padova, Italy.

PMID: 2712828
DOI: 10.1016/0006-291x(89)91637-9

Abstract

In SDS gels caldesmon (Mr = 140 kDa) and myosin light chain kinase (Mr = 130 kDa) migrate as a closely separated doublet. When glycerol is added to the gel caldesmon is characterized by an anomalous migration. In fact under this latter condition, the distance between caldesmon and myosin light chain kinase is enhanced by two-three times. The nature of putative caldesmon and myosin light chain kinase was confirmed by physicochemical, enzymatic and immunological methods.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Calmodulin-Binding Proteins / isolation & purification*
Chickens
Electrophoresis, Polyacrylamide Gel
Gizzard, Avian / analysis
Glycerol
Hot Temperature
Immunoblotting
Muscle, Smooth / analysis
Myosin-Light-Chain Kinase / isolation & purification*
Myosin-Light-Chain Kinase / metabolism
Myosins / metabolism
Phosphorylation

Substances

Calmodulin-Binding Proteins
Myosin-Light-Chain Kinase
Myosins
Glycerol