Bohr effect in Escherichia coli aspartate transcarbamylase. Linkages between substrate binding, proton binding, and conformational transitions.
Journal Article
Overview
publication date
- July 10, 1979
has subject area
- Acids, Acyclic - Phosphonoacetic Acid
- Amino Acids, Acidic - Aspartic Acid
- Amino Acids, Dicarboxylic - Aspartic Acid
- Blood Proteins - Oxyhemoglobins
- Calorimetry
- Carbamates - Carbamyl Phosphate
- Carboxyl and Carbamoyl Transferases - Aspartate Carbamoyltransferase
- Cations, Monovalent - Protons
- Electrochemical Techniques - Potentiometry
- Elements - Protons
- Excitatory Amino Acids - Aspartic Acid
- Gammaproteobacteria - Escherichia coli
- Gases - Protons
- Globins - Oxyhemoglobins
- Gram-Negative Facultatively Anaerobic Rods - Escherichia coli
- Hydrogen-Ion Concentration
- Multifunctional Enzymes - Aspartate Carbamoyltransferase
- Nucleons - Protons
- Organophosphates - Carbamyl Phosphate
- Organophosphonates - Phosphonoacetic Acid
- Photometry - Spectrophotometry
- Protein Conformation
- Spectrum Analysis - Spectrophotometry
- Succinates
- Titrimetry - Potentiometry
has restriction
- closed
Date in CU Experts
- March 13, 2015 12:51 PM
Full Author List
- Allwell NM; Hofmann GE; Zaug A; Lennick M
author count
- 4
published in
- Biochemistry Journal
Other Profiles
International Standard Serial Number (ISSN)
- 0006-2960
Digital Object Identifier (DOI)
Additional Document Info
start page
- 3008
end page
- 3015
volume
- 18
issue
- 14