[Biospecific chromatography of Bacillus subtilis metalloendoproteinase and detection of multiple forms of the enzyme].

Metalloendoproteinase was isolated from protosubtilin, i.e. a mixture of enzymes produced by Bacillus subtilis, during adsorption on activated carbon and a subsequent biospecific chromatography on DNP--hexamethylene diamine--Sepharose 4B and gramicidin S--Sepharose 4B. The molecular weight of the enzyme estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was found to be 36.000. The preparation isolated contained four molecular forms of the enzyme, each splitting DNP-Gly-Gly-Val-Arg. It is shown that thermolysine, purified by biospecific chromatography, consists of three molecular forms. The amino acid composition of metalloendoproteinase was established.