E. Costanzi et al., HEXOSAMINIDASE IN TRICHINELLA-SPIRALIS IS A SINGLE PROTEIN WITH ALPHA-SUBUNIT AND BETA-SUBUNIT CATALYTIC ACTIVITIES, Cellular and molecular biology, 43(6), 1997, pp. 835-840
beta-N-acetylhexosaminidase is expressed as a single protein in Trichi
nella 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 respecti
vely hydrolyzed by the beta- and alpha-subunits. The enzyme is thermos
table, has a basic isoelectric point, and thus is similar to the B iso
enzyme. Northern blotting experiments indicate that the enzyme is enco
ded by a single gene. Hexosaminidase from Trichinella spiralis shows t
hat the substrate specificities of alpha- and beta-subunits precede th
e duplication of their genes.