Separation and properties of human brain hexosaminidase C.
Hexosaminidase C was separated from human brain supernatant by immunoadsorption of the A and B forms on to a column of immobilized antibody followed by preparative starch-block electrophoresis. There were some differences in the properties of hexosaminidase C preparations after each of these stages, shown by comparison of their heat-inactivation characteristics and filtration through Bio-Gel P-200. The C form prepared by both separation steps had properties which differed markedly from those of the A and B isoenzymes; its molecular weight was much larger, greater than 200000, it had optimum activity between pH6 and 7 and could not be successfully eluted from DEAE-cellulose, even with high salt concentrations, or from Sephadex G-200. These results seem to support the proposal that the C form is under a separate genetic control from the others.
D000327:Adsorption; D000818:Animals; D000906:Antibodies; D001921:Brain / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D004592:Electrophoresis, Starch Gel; D005374:Filtration; D006596:Hexosaminidases / Q000302:isolation & purification*; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification; D008970:Molecular Weight; D011817:Rabbits / Q000276:immunology
D000906:Antibodies; D007527:Isoenzymes; D006596:Hexosaminidases