Physico-chemical properties and rheological behaviour of Patella caerula paramyosin.
Paramyosin is a muscle protein which is characteristic of all invertebrates but which is not present in vertebrate muscles. Given the functional importance of paramyosin, the purpose of this paper was to study the physico-chemical properties, including the amino acid composition and rheological behaviour, of purified paramyosin and to investigate its mode of interaction with myosin. Paramyosin was purified from the limpet (Patella caerula) by an ethanol precipitation step. It was soluble at ionic strengths below 0.05 M NaCl and its maximum solubility at neutral pH occurred at approximately 0.4 M NaCl. At this high ionic strength, the pH dependence of solubility was such that paramyosin passed quickly into solution when pH exceeded pH 5, the transitional pH value. By using an immunological method, it was shown that interactions between paramyosin and myosin occurred, even in the presence of actin. The molecular assembly of both proteins was probably specified by hydrophobic interactions, as well as by interactions enhanced by divalent cations. The changes in the dynamic shear storage modulus (G') started between 40 degrees C and 50 degrees C, and reached a maximum at about 75 degrees C.
D000199:Actins / Q000737:chemistry / Q000302:isolation & purification; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001492:Bass; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006863:Hydrogen-Ion Concentration; D008974:Mollusca; D009218:Myosins / Q000737:chemistry / Q000302:isolation & purification; D012212:Rheology; D012995:Solubility; D014335:Tropomyosin / Q000737:chemistry* / Q000302:isolation & purification
D000199:Actins; D000596:Amino Acids; D014335:Tropomyosin; D009218:Myosins