No abstract

No abstract

A protease has been isolated from germinated sorghum seeds in a highly purified, crystalline form. A molecular weight of about 80000 has been obtained for the enzyme from gel filtration experiments. The protease does not require serine or cysteine (sulfhydryl) a t the active site and has no requirement for metal ions. This enzyme has been classified as an "acid protease", since it has its pH optimum a t acidic pH range (pH 3.6). Effects of enzyme concentration and substrate concentration on the rate of catalysis have been studied and an apparent K , of 0.76 mM and 0.19 mM has been obtained against bovine serum albumin and N,N-dimethyl albumin as substrates, respectively. Proteases which possess a high degree of specificity towards peptide bond hydrolysis have played a central role in the determination of the primary structure of proteins [6]. Only a few enzymes can fulfill this role and the search for others with novel specificities has continued. The present paper describes the preparation and enzymological properties of a crystalline acid protease from germinated grain sorghum. The accompanying paper [7] deals with the substrate specificity of the purified protease which has been shown to possess a novel specificity. The enzyme hydrolyzes specifically glutamyl and aspartyl peptide bonds.

No abstract

No abstract