Beta-N-acetylhexosaminidase is expressed as a single protein in Trichinella spiralis and has catalytic properties similar to the alpha- and beta-subunits of human and mouse isoenzymes A and B. It can hydrolyze the artificial substrates, 4-methylumbelliferyl-beta-D-glucosamine and 4-methylumbelliferyl-beta-D-glucosamine-6-sulphate which are respectively hydrolyzed by the beta- and alpha-subunits. The enzyme is thermostable, has a basic isoelectric point, and thus is similar to the B isoenzyme. Northern blotting experiments indicate that the enzyme is encoded by a single gene. Hexosaminidase from Trichinella spiralis shows that the substrate specificities of alpha- and beta-subunits precede the duplication of their genes.
Costanzi, E., Beccari, T., Della Fazia, M., Servillo, G., Orlacchio, A., Tassi, C., et al. (1997). Hexosaminidase in Trichinella spiralis is a single protein with alpha- and beta-subunits catalytic activities. CELLULAR AND MOLECULAR BIOLOGY, 43(6), 835-840.
Hexosaminidase in Trichinella spiralis is a single protein with alpha- and beta-subunits catalytic activities
ORLACCHIO, ANTONIO;
1997-09-01
Abstract
Beta-N-acetylhexosaminidase is expressed as a single protein in Trichinella spiralis and has catalytic properties similar to the alpha- and beta-subunits of human and mouse isoenzymes A and B. It can hydrolyze the artificial substrates, 4-methylumbelliferyl-beta-D-glucosamine and 4-methylumbelliferyl-beta-D-glucosamine-6-sulphate which are respectively hydrolyzed by the beta- and alpha-subunits. The enzyme is thermostable, has a basic isoelectric point, and thus is similar to the B isoenzyme. Northern blotting experiments indicate that the enzyme is encoded by a single gene. Hexosaminidase from Trichinella spiralis shows that the substrate specificities of alpha- and beta-subunits precede the duplication of their genes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
