Abstract
1. 1. Paramyosin was isolated and purified from the molluscan bivalves Crassostrea virginica and Mercenaria mercenaria, the whelk Busycon contrarium and the chiton Acanthopleura granulata. For this purpose, three different extractive procedures were compared. Only paramyosin of the two species of bivalves appeared to be partially degraded if care was not taken to prevent proteolytic attack during the isolation procedure. 2. 2. The molecular weight, electrophoretic behavior, solubility at neutral pH and susceptibility to denaturation by guanidine-HCl were compared for paramyosins from the four species. All were similar in these properties and each was denatured by guanidine-HCl in multiple stages. 3. 3. Paramyosins from the four species wcre compared for susceptibility to proteolysis by pepsin and trypsin. In all cases a proteolysis-resistant segment of 110,000–150,000 Daltons accumulated. These results suggest that regions of paramyosin vary in stability, that these regions are of about the same size for the four species and that the variations of stability may be of physiological significance for function.
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