Aspartate-90 and arginine-269 of hamster aspartate transcarbamylase affect the oligomeric state of a chimaeric protein with an Escherichia coli maltose-binding domain.

Residues Asp-90 and Arg-269 of Escherichia coli aspartate transcarbamylase seem to interact at the interface of adjacent catalytic subunits. Alanine substitutions at the analogous positions in the hamster aspartate transcarbamylase of a chimaeric protein carrying an E. coli maltose-binding domain le...

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Bibliografske podrobnosti
Main Authors: Qiu, Y, Davidson, J N
Format: Artigo
Jezik:Inglês
Izdano: 1998
Teme:
Research Article
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC1219037/
https://ncbi.nlm.nih.gov/pubmed/9425105
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