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Properties of Two Homologous Alkaline Proteases from Streptomyces rectus

^a Department of Microbiology, University of Illinois, Urbana, Illinois 61801

ABSTRACT

Some physicochemical properties of two thermostable proteases from Streptomyces rectus are described. The enzymes were judged to be identical with respect to molecular weight, inactivation with serine protease inhibitors, and in primary structure by peptide analysis. Amino acid analysis indicated the enzymes had identical compositions except for their amide content. The molecular weights of the enzymes were judged to be 28,000 by sedimentation equilibrium, 26,200 by sedimentation diffusion, and 29,100 from amino acid analysis. Titration of the proteases with diisopropylfluorophosphate and phenylmethane sulfonylfuoride indicate equivalent weights of 28,500 and 32,800 g, respectively, for the proteins. The pentapeptide around the serine residue reacting with diisopropylfluorophosphate was isolated and had the composition: Asx₁, Gly₁, Thr₁, Ser₁, Met₁.

¹ Present address: Department of Medical Microbiology, University of California, Irvine, Calif. 92664.

² Present address: University of Delaware, Newark, Del. 19711.