Abstract
Lysozyme/EDTA treatment of four fast-growing rhizobia released repeatable protein profiles after polyacrylamide slab gel electrophoresis. Similar treatment of slow-growing rhizobia failed to release such periplasmic proteins. For the four-fast-growing rhizobia, both P-repressible and P-inducible protein bands occurred. The only P-repressible protein identified was alkaline phosphatase, which showed strain differences in both electrophoretic mobility and activation by Mg2+. The derepression of the P-repressible periplasmic proteins in cowpea Rhizobium NGR234 correlated with derepression of both phosphate and glycerol 1-phosphate uptake.
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