Abstract

Production by normal human erythrocytes of a substrate for cholinesterase has been demonstrated.

At body temperature, the formation and hydrolysis of the cholinesterase substrate is delicately controlled.

At lowered temperatures, 0 to -1.5 C., production of cholinesterase substrate greatly exceeds its hydrolysis.

The quantity of cholinesterase substrate capable of exerting its influence governs the quantity of dextrose converted to lactic acid by the erythrocyte under anaerobic conditions.

The observations corroborate and extend the suggestion of Lindvig, Greig, and Peterson that cholinesterase is part of a cellular system governing erythrocyte permeability.

The balance between production and hydrolysis of cholinesterase substrate at low temperature exhibits the same undulating fluctuations during red cell storage that have been noted for other erythrocyte metabolic functions.

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