Comparison of the property of a novel isozyme E (formerly null mutant, O) with other isozymes of hemolymph acid phosphatase of the silkworm.
1. A novel acid phosphatase isozyme E (formerly null mutant 0) was partially purified by ammonium sulfate fractionation, DEAE-Sephacel and Sephacryl S-200 column chromatography, and its properties were compared with those of other isozymes of the silkworm hemolymph. 2. The isozyme E was extremely heat labile and showed lower pH-stability than those of others. 3. Three isozymes hydrolyzed p-nitrophenyl phosphate, alpha-naphthyl phosphate, alpha-naphthyl phosphate and glucose-1-phosphate strongly. The isozyme E showed about 50% hydrolyzing activity for alpha-naphthyl phosphate as compared to those of A and B. 4. Activities of three isozymes were inhibited by tartaric acid, sodium fluoride, ammonium molybdate and potassium diphosphate. Inhibitory effects of Cu(2+) and HG(2+) were most remarkable against E isozyme.
Department of Applied Biology, Kyoto Institute of Technology, Matsugaski, Japan.
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Horii
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Eguchi
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D002413:Cations, Divalent / Q000494:pharmacology; D006458:Hemolymph / Q000201:enzymology*; D006358:Hot Temperature; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D013379:Substrate Specificity
D002413:Cations, Divalent; D007527:Isoenzymes; D000135:Acid Phosphatase