Dataset Information


Separation and properties of human brain hexosaminidase C.

ABSTRACT: 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.

SUBMITTER: Braidman I 

PROVIDER: S-EPMC1168384 | BioStudies | 1974-01-01

SECONDARY ACCESSION(S): 10.1042/bj1430295

REPOSITORIES: biostudies

Similar Datasets

1976-01-01 | S-EPMC1164150 | BioStudies
1976-01-01 | S-EPMC1172820 | BioStudies
1973-01-01 | S-EPMC1165847 | BioStudies
1975-01-01 | S-EPMC1165192 | BioStudies
1978-01-01 | S-EPMC1185762 | BioStudies
1981-01-01 | S-EPMC1163082 | BioStudies
1977-01-01 | S-EPMC1183623 | BioStudies
1972-01-01 | S-EPMC1174318 | BioStudies
1977-01-01 | S-EPMC1164867 | BioStudies
1981-01-01 | S-EPMC1162582 | BioStudies