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J Bacteriol. 1971 August; 107(2): 461-467
Copyright © 1971 American Society for Microbiology. All Rights Reserved.
a Department of Biology, Biological Research Laboratories, Syracuse University, and the Department of Microbiology, Upstate Medical Center, State University of New York, Syracuse, New York 13210
ABSTRACT
Immunochemical properties of L-asparaginases from Serratia marcescens and Escherichia coli were compared by means of quantitative precipitin reactions and quantitative microcomplement-fixation reactions employing homologous and heterologous antisera. The enzyme preparations used in these tests produced one arc of precipitate upon immunoelectrophoresis. According to our results with the precipitin and micro-complement fixation reactions, both enzymes are related immunochemically. On the basis of these tests, distinct structural differences exist between the two enzymes. From results with the micro-complement fixation test, we estimated that the two enzymes could differ by 10 to 15 amino acid residues.
2 Present address: Shell Development Co., Modesto, Calif.
1 This report was presented in part at the 69th Annual Meeting of the American Society for Microbiology, Miami Beach, Fla., 49 May 1969.
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