マサバ血合肉中のイノシン酸分解酵素の分離・精製及びその諸性質

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It has been shown that the rapid degradation of inosinic acid (IMP) in the dark muscle of common mackerel Scomber japonicus is possibly catalized by an enzyme having high activity at pH 6.0. The enzyme was extracted from acetone powder and purified by the two steps of affinity chromatography on Concanavalin A-Sepharose and DEAE-cellulose chromatography. The purified enzyme was shown to be homogeneous by disc polyacrylamide gel electophoresis and its molecular weight was estimated to be about 9×104 by gel filtration. The enzyme was identified as acid phosphomonoesterase (EC 3.1.3.2), since it hydrolyzed 5'-IMP optimally at pH 5.5 and hydrolyzed various phosphorylated compounds including 5'-nucleotides, 3'-nucleo-tides, glucose-6-phosphate, β-glycerophosphate and p-nitrophenyl phosphate (p-NPP). The enzyme was inhibited by Cu2+, Zn2+, Fe2+ and NaF, but was not affected by Mg2+, Mn2+, Co2+, Ni2+, Ca2+, EDTA and iodoacetic acid. The presence of the other acid phosphatase which hydrolyzes p-NPP but not 5'-IMP was presumed in an unadsorbed fraction to Concanavalin A-Sepharose.
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