THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE

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Abstract
Renin substrate from multiple 50 gal lots of hog plasma, after (NH4)2SO4 fractionation and partial acid denaturation, was given a batch DEAE cellulose treatment. DEAE column chromatography next resolved the activity into 3 major (A, B and C) and 2 minor components. A, B and C were partitioned in polyethylene glycol-Na2SO4 systems; then B and C, but not A, each gave 2 more active forms (B1, B2; C1C2) on countercurrent distribution in an analogous Li2SO4 system. Migrations vs hog serum, observed in paper and starch gel electrophoresis, were A, between [alpha]2 and [beta] globulin; B1 and B2, trailing [alpha]2; and C1 and C2, coinciding with [alpha]2. Impurities in B1 and B2 precluded further analysis. Ultracentrifuge mol wts for A, C1 and C2 were 57,200, 57,700 and 55,600. All 3 had nearly identical amino acid compositions and contained N terminal aspartic acid plus varying amounts of sialic acid, glucosamine and hexose. The maximum Goldblatt units per mg were A, 25.7; C1, 12.2; and C2, 14.5. All appeared to yield the same angiotensin at the same rate, using hog renin.