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. 1975 Sep;123(3):1000–1005. doi: 10.1128/jb.123.3.1000-1005.1975

Soluble and membrane-bound aspartate-binding activities in Salmonella typhimurium.

R R Aksamit, B J Howlett, D E Koshland Jr
PMCID: PMC235825  PMID: 239919

Abstract

The specificities of the soluble and membrane aspartate-binding activities were compared with each other and with the specificity of aspartate chemotaxis and were found to be distinct. The soluble aspartate-binding protein was purified to homogeneity and had a molecular weight of 30,000. The dissociation constant was 10(-6) M for aspartate, and the protein bound glutamate, cysteic acid, and 2-amino-3-phosphonopropionate. Aspartate transport was inhibited by cysteic acid.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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