Open AccessHuman kidney hexosaminidase A and hexosaminidase B form a complex
Author(s) -
PSHEZHETSKY Alexey V.,
BUNEEVA Olga A.,
DVORKIN Vladimir M.
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16383.x
Subject(s) - hexosaminidase , kidney , chemistry , enzyme , supramolecular chemistry , biochemistry , biology , crystallography , endocrinology , crystal structure
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.