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- W2064178103 abstract "An acidic β-galactosidase was purified approximately 2,500-fold to homogeneity from the shrimp Penaeus japonicus. with a final specific activity of 4,000 units/mg of protein. SDS-polyacrylamide gel electrophoresis revealed the monomers of the acidic β-galactosidase to have a relative mass of 66,000. Since the active acidic β-galactosidase was found to have a relative mass of 140,000 by Ferguson plot analysis, the purified enzyme was concluded to be dimeric. No protective polypeptide was identified in the final preparation of purified β-galactosidase. The shrimp enzyme was found to be thermolabile. Upon heating at 56°C for 10 min, the enzyme lost 50% of its activity. The acidic β-galactosidase had an isoelectric point (pI) of 4.6 ± 0.1 and the enzyme was sialyated. The shrimp enzyme had a pH optimum of 5.5 and its Km was 43 μM with 4-methylumbelliferyl-β-D-galactoside as substrate. The enzyme was inhibited by both Mn++ and Zn++ ions." @default.
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- W2064178103 date "1991-07-01" @default.
- W2064178103 modified "2023-09-26" @default.
- W2064178103 title "Purification and characterization of an acidic β-galactosidase from the hepatopancreas of the shrimpPenaeus japonicus (Crustacea: Decapoda)" @default.
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- W2064178103 doi "https://doi.org/10.1002/jez.1402590105" @default.
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