Open AccessAmino acid composition and N‐terminal sequence of the NADP‐linked glutamate dehydrogenase from Trypanosoma cruzi
Author(s) -
Cazzulo Juan José,
Nowicki Cristina,
Santome JoséA.,
Wernstedt Christer,
Hellman Ulf
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb03180.x
Subject(s) - glutamate dehydrogenase , biochemistry , biology , neurospora crassa , amino acid , enzyme , escherichia coli , peptide sequence , protein subunit , trypanosoma cruzi , glutamate synthase , microbiology and biotechnology , glutamate receptor , gene , parasite hosting , receptor , world wide web , mutant , computer science
The NADP‐linked glutamate dehydrogenase (NADP‐GDH) from epimastigotes of Trypanosoma cruzi , Tul 2 stock, has been purified by an improved procedure. The enzyme has subunit molecular weight (47 kDa), amino acid composition and N‐terminal sequence similar to those of the NADP‐GDH from Escherichia coli , including the N‐terminal extension of 15 amino acids present in the E. coli enzyme, but not in the NADP‐GDH from Neurospora crassa .