Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00817a009
Reference15 articles.
1. Kritische Untersuchungen über die Grenzen der Anwendbarkeit der Methode der kontinuierlichen Variationen nach Job
2. Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits
3. Aspartate Transcarbamylase
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1. Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase;Archives of Biochemistry and Biophysics;2012-03
2. Aspartate Transcarbamylase from Escherichia Coli: Activity and Regulation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Site-directed alterations to the geometry of the aspartate transcarbamoylase zinc domain: Selective alteration to regulation by heterotropic ligands, isoelectric point, and stability in urea;Biochemistry;1993-04-27
4. Characterization of Coxiella burnetii pyrB;Annals of the New York Academy of Sciences;1990-06
5. Assessment of the number of nucleotide binding sites on chloroplast coupling factor 1 by the continuous variation method;Biochemistry;1988-09-06
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