Abstract
Two maximum points were observed to exist on the solubility curves of fish muscle protein extracted with various salt solutions of different concentrations. Two peaks were also found on the coagulation-temperature curves for the fish muscle solutions extracted with salt solutions of the concentrations at which the solubility curve reached the maximum points. These results suggest two different protein-complexes to exist in a fish muscle. Estimating from the coagulation temperatures of these two proteins, one of them comes under what Furth called a soluble myogenfibrin, and the other corresponds to a myogen. The former protein is much contained in salt solutions of higer concentrations. This fact may be attributed either to the situation that this protein-complex is originally pr_??_sent in any fish muscle and is particularly liable to be extracted with salt solutions of higher concentrations, or to that it is derived secondarily from myogen under influence of salt solutions of higher concentrations. The effect of various ions examined on the solubility of fish muscle proteins was found to follow the Hofmeister series as follows: I'>Br'>Cl'>SO4 in anion, Li ?? >Na ?? >K ?? and Ca¨>Mg¨>Sr¨>Ba¨ in cation.
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