Solubilization and Partial Purification of Amino Acid-Specific Components of the D-Lactate Dehyrogenase-Coupled Amino Acid-Transport Systems*
AUTOR(ES)
Gordon, Adrienne S.
RESUMO
A protein-containing fraction has been solubilized from E. coli ML 308-225 membrane vesicles that has many of the properties of the amino acid “carrier proteins” of the D-lactate dehydrogenase-coupled amino acid-transport systems. Membrane vesicles were partially solubilized with the nonionic detergent Brij 36-T, and the solubilized material was fractionated by Sephadex G-100 chromatography in the presence of the same detergent. Three fractions possess binding activity for proline: one of relatively low molecular weight with a high specific activity, and two of higher molecular weight with low specific activities. The higher molecular weight fractions exhibit D-lactate dehydrogenase activity; however, there is no corresponding activity associated with the low molecular weight fraction. Moreover, proline-binding activity is highly specific as it is not inhibited by structurally-unrelated amino acids. In addition to proline, the low molecular weight fraction exhibits binding activities for serine, glycine, lysine, and tyrosine.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=426457Documentos Relacionados
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