Caldesmon: anomalous electrophoretic behaviour in polyacrylamide gel.
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.
Cavanni
P
P
Institute of General Pathology, University of Padova, Italy.
Cavallini
P
P
Ratti
E
E
Gaviraghi
G
G
Dalla Libera
L
L
D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000302:isolation & purification*; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D005895:Gizzard, Avian / Q000032:analysis; D005990:Glycerol; D006358:Hot Temperature; D015151:Immunoblotting; D009130:Muscle, Smooth / Q000032:analysis; D009219:Myosin-Light-Chain Kinase / Q000302:isolation & purification* / Q000378:metabolism; D009218:Myosins / Q000378:metabolism; D010766:Phosphorylation
D002148:Calmodulin-Binding Proteins; D009219:Myosin-Light-Chain Kinase; D009218:Myosins; D005990:Glycerol