Hexosaminidases A and B from human kidney cortex were purified to homogeneity (concanavalin A affinity chromatography, ion-exchange chromatography and gel filtration). The yield of homogeneous isoenzymes improved about 20-fold, giving preparations of hexosaminidases A and B with specific activities of about 200 and 325 units/mg of protein respectively. The kinetic and structural properties of kidney hexosaminidase isoenzymes were studied and compared with the hexosaminidase isoenzymes from human placenta. The amino acid composition of hexosaminidase A was significantly different from that of hexosaminidase B. In the event of success in developing enzyme-replacement therapy for Tay-Sachs and Sandhoff's diseases, this modified procedure can furnish larger amounts of homogeneous isoenzymes.
|Original language||English (US)|
|Number of pages||5|
|State||Published - 1977|
ASJC Scopus subject areas