English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In the preceding papers (1, 2), we have shown that lipid A, fatty acids, and their derivatives inhibit the accumulation of succinate or amino acids by membrane vesicles from Escherichia coli W2252, which couples to the oxidation of electron donors. We found that the inhibition of transport activities by lipid A and fatty acids was due to the action of these compounds as proton conductors on membrane vesicles and that this inhibition was partly overcome by the addition of bovine serum albumin which could remove these inhibitors from membrane vesicles (3). We also noticed that bovine serum albumin stimulated amino acid transport activities (serine, alanine, glycine, glutamate, leucine, and phenylalanine) of membrane vesicles (3), which was in agreement with the observation of MlzusHIMA (4). We report here a further study on the stimulative effect of bovine serum albumin on the transport activity of serine in membrane vesicles from E, toll W2252. The effect of bovine serum albumin on the removal of lipid materials from membrane vesicles was studied. 14C-acetate-labeled membrane vesicles (0.4 mg protein, and the labeling procedure is given in the legend to Table 1) were diluted to 200 μl final volume containing in final concentrations, 0.05 M potassium phosphate buffer (pH 6.6), 0.01 M MgSO4, and 1.8% bovine serum albumin (Sanko Pure Chemicals Co., Tokyo). The mixture was incubated at 25° for 15 min and diluted with 0.5 ml of 0.05 M potassium phosphate buffer (pH 6.6). It was filtered through a Millipore HAWP membrane filter. The filter was washed twice with 0.5 ml of the same buffer. The radioactivities of the filter and filtrate were measured as described previously (1). It was found that 7 to 10% of the total radioactivity was removed from the membrane vesicles by bovine serum albumin and appeared in the

STIMULATIVE EFFECT OF BOVINE SERUM ALBUMIN ON THE TRANSPORT ACTIVITY OF SERINE IN MEMBRANE VESICLES FROM ESCHERICHIA COLI