Purification of yeast hexokinase and its reaction with ββ′-dichlorodiethyl sulphide

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Abstract
The purification and crystallization of hexokinase from baker''s yeast were described. The addition of cysteine or NaSH to autolyzed yeast, accelerated the liberation of hexokinase and retarded inactivation. The pure enzyme was stabilized by glucose, activated by Mg, and inhibited by SH poisons. Vesicant activity was accompanied by inactivation of hexokinase in vivo. Using mustard gas with radioactive S, it was shown that the sensitivity of hexokinase was not due to any special reactivity but to the dependance of enzyme activity on easily substituted groups.

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