Premium
Evidence for NADH‐ and NADPH‐linked Glutamate Dehydrogenases in Trypanosoma cruzi Epimastigotes *
Author(s) -
WALTER ROLF D.,
EBERT FRANK
Publication year - 1979
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1979.tb04214.x
Subject(s) - biochemistry , glutamate dehydrogenase , enzyme , trypanosoma cruzi , isoelectric point , nadh dehydrogenase , dehydrogenase , nad+ kinase , purine , biology , nucleotide , chemistry , glutamate receptor , protein subunit , gene , world wide web , computer science , parasite hosting , receptor
SYNOPSIS Two glutamate dehydrogenases, NADH‐linked (EC 1.2.1.2) and NADPH‐linked (EC 1.2.1.4.) were isolated from the epimastigote forms of Trypanosoma cruzi and purified. Both enzymes exist as hexamers. The molecular weights of the native NADH‐and NADPH‐linked glutamate dehydrogenases were estimated to be 360,000 and 265,000, respectively, and those of the subunits to be 58,000 and 43,000, respectively. The isoelectric point of the NADH‐linked dehydrogenase is at pH 5.25 and that of the NADPH‐linked enzyme at pH 5.1. The activities of both enzymes are regulated by product inhibition. In addition, purine nucleotides were shown to be potent inhibitors of the NADH‐linked glutamate dehydrogenase.