Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.

Large changes in solvent accessibility to aspartate transcarbamylase (aspartate carbamoyltransferase, carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2), as monitored by tritium exchange, result from binding of substrates and substrate analogs to the catalytic subunit (c3), binding of...

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Hlavní autoři: Lennick, M, Allewell, N M
Médium: Artigo
Jazyk:Inglês
Vydáno: 1981
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC349129/
https://ncbi.nlm.nih.gov/pubmed/7031660
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