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. 1967 Jul;15(4):738–743. doi: 10.1128/am.15.4.738-743.1967

Elution of Loosely Bound Acid Phosphatase from Staphylococcus aureus1

F J Malveaux 1, C L San Clemente 1
PMCID: PMC547050  PMID: 6049297

Abstract

Strains of Staphylococcus aureus from the International-Blair and the Seto-Wilson series of phage propagating strains were examined for acid phosphatase activity. This enzyme was found to occur in varying amounts in three different fractions: free (6 to 60%), loosely bound (25 to 82%), and firmly bound (0 to 46%). Propagating strain 3A, because of its high activity, was chosen for further study. The rate of enzyme production paralleled cell growth in Trypticase Soy Broth, but followed a biphasic pattern in a semisynthetic casein acid-hydrolysate medium with glyceryl phosphate. Maximal elution of acid phosphatase in the loosely bound fraction, presumably from the surface of cells, occurred in the alkaline pH range. From log-phase cells, elution was maximally effected with buffered 1.0 M KCl (pH 7.5), but stationary-phase cells required twice the concentration of KCl.

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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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