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. 1968 Oct;96(4):1357–1365. doi: 10.1128/jb.96.4.1357-1365.1968

Cytochemistry of Phosphatases in Myxococcus xanthus

Herbert Voelz a, Raoul O Ortigoza a,1
PMCID: PMC252457  PMID: 4234839

Abstract

An Mg2+-dependent and a K+-stimulated adenosine triphosphatase were localized by cytochemistry at or near both surfaces of the cytoplasmic membrane of Myxococcus xanthus. An alkaline and an acid phosphatase resided at the external surface of the membrane or in the periplasm. All enzymes could be extracted from partially fixed cells with Mg2+-deficient buffers. Suboptimal external phosphate elicited dissociation of adenosine triphosphatase from the membrane but not that of the unspecific phosphatases. The dissociated enzymes migrated into the cytoplasm where they were associated mainly with cytoplasmic aggregates.

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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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