Apparent negative co-operativity and substrate inhibition in overexpressed glutamate dehydrogenase from Escherichia coli
Author:
Publisher
Oxford University Press (OUP)
Subject
Genetics,Molecular Biology,Microbiology
Link
http://academic.oup.com/femsle/article-pdf/281/2/132/19433127/281-2-132.pdf
Reference24 articles.
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2. A thermally sensitive loop in clostridial glutamate dehydrogenase detected by limited proteolysis;Aghajanian;J Biol Chem,2003
3. The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during reductive amination;Basso;Eur J Biochem,1995
4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford;Anal Biochem,1976
5. The mechanism of substrate inhibition of palmityl coenzyme A: carnitine palmityltransferase by palmityl coenzyme A;Bremer;J Biol Chem,1967
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