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Renin prepared in batches by the DEAE process, followed by ammonium sulfate fractionation and dialysis at pH 5.0, yielded four separate active bands when chromatographed on DEAE in a descending pH gradient. These forms, numbered I through IV, eluted at the characteristic pH values of 5.2, 4.7, 4.5, and 4.25, respectively. When the ammonium sulfate and dialysis steps of the renin preparation were carried out at pH values above 7.0, only renin I was obtained. Dialysis of this chromatographically homogeneous renin I at pH 5.0 or treatment with acid yielded a single renin II component with a remarkably high specific activity.All four forms of renin exhibited similar Michaelis constants, and it is not known whether the forms result from alterations in the enzyme molecule or from association with carrier proteins.The reactions of renin I with pure substrates A, B1, B2, C1, C2, and the tetradecapeptide substrate have been studied. The Michaelis constants obtained were similar, and ranged from 0.71 to 1.76 × 10 moles per liter.