Purification and properties of caldesmon-like protein from molluscan smooth muscle.
In this comparative study, the heat-stable protein content of scallop muscles was reinvestigated. The hCaD-like protein was prepared and its properties carefully examined. The heat-stable high-molecular-mass caldesmon-like (hCaD-like) protein is only present in the catch (smooth) muscle and it is completely absent in the striated muscle of scallop. The isolated scallop hCaD-like protein cosediments with F-actin, binds to myosin significantly and inhibits the ATPase activity of acto-myosin. A partial cDNA clone from a Mytilus anterior byssus retractor muscle (ABRM)-related protein showed strong homology with the hCaD gizzard sequence. This allowed identification of the heat-stable 100-110 kDa protein doublet band isolated in this study as a caldesmon-like molecule.
Csizmadia
A M
AM
Department of Biochemistry, Eötvös Lorand University, Budapest, Hungary.
Bonet-Kerrache
A
A
Nyitray
L
L
Mornet
D
D
D000595:Amino Acid Sequence; D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D002645:Chickens; D003001:Cloning, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008974:Mollusca / Q000737:chemistry* / Q000235:genetics; D009124:Muscle Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D009130:Muscle, Smooth / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D002148:Calmodulin-Binding Proteins; D009124:Muscle Proteins