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J Bacteriol. 1969 March; 97(3): 1209-1214
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Staphylococcal Acid Phosphatase: Extensive Purification and Characterization of the Loosely Bound Enzyme1

F. J. Malveaux2 and C. L. San Clemente

a Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan 48823

ABSTRACT

Acid phosphatase of Staphylococcus aureus PS55 was eluted from the surface of these cells with 1.0 M KCl at pH 8.5 by gentle agitation at 25 C and was purified 44-fold (51% recovery) by two cycles of dialysis and gel filtration. The eluted enzyme which had a 280/260 (nm) absorbancy ratio of 0.71 required at least 0.5 M salt solution for solubilization; however, most of the purified product which had a 280/260 (nm) absorbancy ratio of 1.72 was soluble in dilute buffer solution [0.01 M tris(hydroxymethyl)aminomethane chloride, pH 8.5]. Purified acid phosphatase appeared homogeneous according to the criteria of gel filtration, starch-block electrophoresis, and analytical ultracentrifugation. In a starch block, migration was toward the cathode at pH 8.0. Maximal activity occurred at pH 5.2 to 5.3 and salt concentration had little effect on phosphatase activity up to 1.0 M KCl or NaCl. Progressive loss of enzymatic acitivity occurred at higher salt concentrations. Molecular weight of purified acid phosphatase was estimated to be 58,000.

FOOTNOTES

2 Present address: Department of Microbiology, College of Medicine, Howard University, Washington, D.C. 20001.

1 Published with the approval of the Director of the Michigan Agricultural Station as Journal Article no. 4542.

J Bacteriol. 1969 March; 97(3): 1209-1214
Copyright © 1969 American Society for Microbiology. All Rights Reserved.





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