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IT is clear that, for the determination of enzymic reaction-velocity under readily definable conditions, the states near the initiation of the reaction are decidedly the best. Usually however this part of the progress has been left unexplored and delineation of it has been based merely upon empirical expressions of doubtful value. In the present paper data have been directly collected within a few minutes of the origination of the reaction on the mixing of enzyme and substrate. From these data "initial slopes"' are determined graphically and used as a measure of reaction-velocity. In experiments of this short duration the difference between apparent and true zero-time becomes significant. THE STARCH-AMYLASE SYSTEMI. DESCRIPTION OF AN "INITIAL SLOPE MIETHOD.

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The general mechanism for enzymic group-transfer reactions is shown to be of considerable complexity. In order to deal with this complexity, an analysis has been made of the structure of steady-state rate equations, which permits the establishment of direct relationships between specified features of mechanism and of rate behavior. This has opened up the possibility of a featurewise approach for the progressive elucidation of complex enzymic mechanisms. In particular, a theoretical basis has been provided for the comprehensive consideration and systematic differentiation of mechanisms of enzymic group-transfer reactions.