Kinetics of the renin-substrate reaction employing a synthetic substrate

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Abstract
The kinetics of the renin-substrate reaction, employing a synthetic tetradecapeptide substrate, were investigated. Hog renin was shown to cause a splitting of the peptide at the leucyl10-leucine11 bond with the subsequent formation of angiotensin I and a 4-amino acid fragment. The reaction was shown to exhibit 1st-order kinetics and a pH optimum of 6.5-7.0. The yield of angiotensin I following a fixed period of incubation was proportional to the amount of enzyme added. Incubations carried out in a Ringer-Krebs solution demonstrated that the ionic composition of plasma has no marked effect on the kinetics of this reaction.