Studies of lysosomal enzymes in fish muscle tissue. VIII Chracterization of neutral .BETA.-N-acetylglucosaminidase in carp blood.

The purified carp blood neutral β-N-acetylglucosaminidase has been distinguished. The enzyme had a pH optimum of 6.5, but it was quite stable in pH range from 7.0 to 11.0. The enzyme was heat-labile and lost more than 90% of the activity when preincubated at 50°C for 10min. The enzyme was stimulated by dithiothreitol and 2-mercaptoethanol at a concentration of about 10mM and not inhibited by free N-acetylgalactosamine or acetate. Inhibition by divalent metal ions increased in the order of Mn2+

Keywords:

• Enzyme
• Dithiothreitol
• Biochemistry
• Substrate (chemistry)
• Isoelectric point
• Divalent
• Chemistry
• Glycerol
• Size-exclusion chromatography
• Carp
• Muscle tissue

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