スルメイカのトリニトロフェニル化ミオシンの酵素的性質とキモトリプシン消化性

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Squid mantle myosin was trinitrophenylated with 2, 4, 6-trinitrobenzene sulfonate and squid trinitrophenyl myosin, in which approximately one mol of trinitrophenyl group bound to 2.4×105g of myosin was thus obtained. The Ca-, EDTA-, and Mg-ATPase activities of squid trinitrophenyl myosin were practically identical to those of squid unmodified myosin in the KCI-concentration dependence, in the temperature dependence, and in the effect of thiol modification, although specific activities of the three ATPases were all affected. The thermostability of Ca-ATPase activity of squid myosin was also unaltered by trinitrophenylation of myosin. These results suggested that the trinitrophenylation of squid myosin caused no change in the bulk conformation of squid myosin molecule. The effect of the α-chymotryptic digestion on the three ATPase activities was enhanced by trinitrophenylation of myosin, and even further enhanced when trinitrophenylation was conducted in the presence of PPi. Analysis of the digested products by SDS gel electrophoresis revealed that the yield of subfragment-1 from the chymotryptic digestion decreased by tirnitrophenylation of myosin, and decreased even further when trinitrophenylation was conducted in the presence of PPi.It is therefore suggested that the reactive lysine residues trinitrophenylated in the presence of PPi are located closer to the ATPase active site than those of trinitrophenylated in the absence of PPi and that the chymotryptic cleavage at the site within subfragment-1 was enhanced by trinitrophenylation.
社団法人日本水産学会の論文

スルメイカのトリニトロフェニル化ミオシンの酵素的性質とキモトリプシン消化性

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