Human kidney hexosaminidase A and hexosaminidase B form a complex.
The isolation and purification of human kidney hexosaminidases A and B was carried out. Regulation of the supramolecular organization and catalytic activity of hexosaminidases was investigated in the bis(2-ethylhexyl)sulphosuccinate reversed micellar system modeling the enzyme microenvironment in the lysosomes. It was shown that hexosaminidases A and B associate forming 280-300-kDa dimeric complexes under these conditions. At pH 4.75, the hexosaminidases A and B can be isolated from kidney tissue only in the form of this complex.
Pshezhetsky
A V
AV
Belozersky Laboratory, Moscow State University, USSR.
Buneeva
O A
OA
Dvorkin
V M
VM
D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D054818:Hexosaminidase A; D054819:Hexosaminidase B; D006801:Humans; D007668:Kidney / Q000201:enzymology*; D008823:Micelles; D014461:Ultracentrifugation; D001619:beta-N-Acetylhexosaminidases / Q000302:isolation & purification / Q000378:metabolism*
D008823:Micelles; D054818:Hexosaminidase A; D054819:Hexosaminidase B; D001619:beta-N-Acetylhexosaminidases