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J Bacteriol. 1971 March; 105(3): 957-967
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Use of Antibody to Membrane Adenosine Triphosphatase in the Study of Bacterial Relationships¹

^a Department of Microbiology, New York University, School of Medicine, New York, New York 10016

ABSTRACT

An antiserum to Ca²⁺-activated adenosine triphosphatase from membranes of Micrococcus lysodeikticus cross-reacted in agar gels with membrane adenosine triphosphatases from other pigmented micrococci and related species. Species of Micrococcus and Sarcina showed different levels of inhibition of adenosine triphosphatase activities in heterologous reactions with antiserum. Inter- and intraspecific relationships based on the inhibition reaction were compared with an independent parameter, namely the quantitative and qualitative composition of the bacterial membrane phospholipids and fatty acids. The guanine plus cytosine contents in the deoxyribonucleic acid of the species studied correlated well with the serological cross-reactivity of adenosine triphosphatases from their membranes. The types of cross-bridges found in the peptidoglycans of these cocci were also compared with the other properties. The results suggest that an antiserum specific for a major membrane protein may be a reliable and most useful adjunct in studying bacterial serotaxonomy.

² Present address: Department of Microbiology, University of Maine, Orono, Me. 04473.

¹ This paper was presented in part at the 70th Annual Meeting of the American Society for Microbiology, Boston, Mass., 26 April—1 May, 1970.