貝類蛋白質の研究-IV : 熱非凝固区分について

概要

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Non-heat-coagulable protein was isolated from muscle extracts of Meretrix meretrix, Mactra sulcataria, and Atrina Japonicum, respectively. Content of this proteinous material in muscle as well as contents of nitrogen and reducing substance in the material was estimated (Table 1). The paper-electrophoretic analysis revealed that the material consisted at least of three subfractions with different mobilities. From these three, one having zero mobility was precipitated with acetic acid. It was found furthermore that the heat-coagulable components of muscle extracted with a buffer solution of low ionic strength (μ=0.1, pH 7.8)turned noncoagulable when dialyzed for short time (about 3 hours) against the same buffer solution as the above extractant. Whereas the paper-electrophoretic behaviours remained unchanged after such dialysis, the coagulability of these comppnents changed to a high degree. These non-coagulable matters were found to be of low mobility, while the coagulated porteins showed no mobility as expected. Molecular event leading to the said loss of coagulability is not clear as yet, though the loss seems to be connected mcre or less intimately with pH of the dialysate.
公益社団法人日本水産学会の論文