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PMID: 2712828 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Caldesmon: anomalous electrophoretic behaviour in polyacrylamide gel.

Biochemical and biophysical research communications ·Vol. 160 ·No. 1 ·1989-04-14 ·Pages 174-80

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

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.

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,metabolism Myosins/metabolism Phosphorylation
Chemicals
Calmodulin-Binding Proteins Myosin-Light-Chain Kinase Myosins Glycerol
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Cavanni P
Institute of General Pathology, University of Padova, Italy.
Cavallini P
Ratti E
Gaviraghi G
Dalla Libera L
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1989-04-14
Pages
174-80
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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