Nov 1, 1975

Inhibitory effect of dioctyl sodium sulfosuccinate on trypsin activity

Journal of Pharmaceutical Sciences
G S JodhkaS A Knalil

Abstract

The inhibitory effect of dioctyl sodium sulfosuccinate on the proteolytic activity of trypsin was investigate over the pH 6-8 range. The antitryptic activity was determined using two different substrates: casein and N,alpha-benzoyl-DL-arginine-p-nitroanilide hydrochloride. The mechanistic studies revealed the substrate-inhibitor interaction to be the overall major mechanism of inhibition. This interaction was shown to involve substrate depletion, probably involving some primary sites of the natural substrate casein. Some inhibition was also shown to be due to an interaction between the enzyme and the inhibitior molecules. The interactions of the inhibitor with the enzyme and the substrate were irreversible. The possible therapeutic significance of the inhibitory effect of the surfactant is discussed.

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References

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Citations

Mentioned in this Paper

Casein allergenic extract
Caseins
Surfactant [EPC]
Endogenous Surfactants
Trypsin Inhibitors
Pulmonary Surfactants
Proteolytic Enzyme
Plasma Protein Binding Capacity
Trypsin
Arginine

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