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Interaction of α2-macroglobulin with alkaline proteinase from an alkalophilicBacillus sp. grown in an extraordinarily alkaline environment

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Abstract

The interaction of α2-macroglobulin (α2M) with an alkaline serine proteinase (ALPase I) from alkalophilicBacillus sp. grown in an extraordinarily alkaline environment was investigated. Stoichiometry of the reaction showed that ALPase I bound to α2M in a molar ratio of about 2∶1. The α2M-ALPase I complex showed about 80% of the proteinase activity shown by ALPase I in the hydrolysis of succinyl-l-alanyl-l-alanyl-l-prolyl-l-phenylalanyl-4-methyl-coumaryl-7-amide (Suc-Ala-Ala-Pro-Phe-MCA) and casein. The conformational changes in the α2M molecule caused by the complex formation at pH 7.5 were determined from electron micrographs and difference spectra. The antigenic activity of the α2M-ALPase I complex with the anti-ALPase I antiserum was found to be completely abolished. Immunoelectrophoresis of the complex incubated at pH 7.5 after 48 h showed no appreciable change, and the complex was recognized as exhibiting enhanced stability at pH 7.5.

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Authors and Affiliations

  1. Laboratory of Molecular Enzymology, Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, 1-1, Tsutsumidori-Amamiyamachi, 981, Sendai, Japan

    Youhei Yamagata &  Eiji Ichishima

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  1. Youhei Yamagata
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  2. Eiji Ichishima
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Yamagata, Y., Ichishima, E. Interaction of α2-macroglobulin with alkaline proteinase from an alkalophilicBacillus sp. grown in an extraordinarily alkaline environment. Current Microbiology 27, 205–209 (1993). https://doi.org/10.1007/BF01692877

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