Am. Csizmadia et al., PURIFICATION AND PROPERTIES OF CALDESMON-LIKE PROTEIN FROM MOLLUSCAN SMOOTH-MUSCLE, Comparative biochemistry and physiology. B. Comparative biochemistry, 108(1), 1994, pp. 59-63
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 ca
ldesmon-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, bind
s to myosin significantly and inhibits the ATPase activity of acto-myo
sin. A partial cDNA clone from a Mytilus anterior byssus retractor mus
cle (ABRM)-related protein showed strong homology with the hCaD gizzar
d sequence. This allowed identification of the heat-stable 100-110 kDa
protein doublet band isolated in this study as a caldesmon-like molec
ule.