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| Content Provider | Journal of Biological Chemistry (JBC) |
|---|---|
| Author | Wilson, Onslow H. Holden, Joseph T. |
| Abstract | Cold osmotic shock treatment of early stationary phase Escherichia coli W cells reduced the capacity for arginine uptake and accumulation by about 25%. DEAE-cellulose chromatography of the shock fluid separated four protein-containing fractions having relatively specific arginine-binding activity. The reduced transport activity of shocked cells was partially restored by two of these purified protein fractions (I and III). The degree of restoration was linear between 5 and 10 µg per ml for Fraction I; above 10 µg per ml there was a marked reduction in the extent of stimulation. For Fraction III restoration of the initial rate (15 sec) was a curvilinear function of the protein concentration from 5 to 40 µg per ml. The degree of restoration of the steady state level of uptake (5 min) hardly changed within this protein concentration range. Fractions I and III have identical dissociation constants for arginine, the values ranging from 0.5 to 1 x 10-6 m.14C-Arginine was not metabolized by concentrated crude shock protein. The material bound by this protein solution and by purified Fractions I and III was found to have the same Rf value as free arginine.Analysis of the intracellular pool radioactivity after exposure of shocked cells to 14C-arginine and to 14C-arginine plus optimal concentrations of Fractions I and III (in the presence of 4 x 10-3 m amineoxyacetic acid) showed that the bulk of the radioactivity (∼90%) remained in arginine, thereby showing that these proteins stimulate the arginine accumulation process. The proteins are specific in binding and stimulating the transport of arginine. They bound little or no lysine and canavanine and did not stimulate the transport of lysine in shocked cells.These data suggest that cold osmotic shock treatment of E. coli W releases proteins which may participate in the accumulation of arginine by these cells, and that these proteins are not capable of functioning in the accumulation of lysine. |
| Related Links | http://www.jbc.org/content/244/10/2743.abstract |
| Ending Page | 2749 |
| Starting Page | 2743 |
| Page Count | 7 |
| File Format | HTM / HTML PDF |
| ISSN | 00219258 |
| Journal | Journal of Biological Chemistry (JBC) |
| Issue Number | 10 |
| Volume Number | 244 |
| e-ISSN | 1083351X |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 1969-05-25 |
| Access Restriction | Open |
| Subject Keyword | CHEMISTRY AND METABOLISM OF SUBSTANCES OF LOW MOLECULAR WEIGHT |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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