Abstract
The adsorption of pepsin, trypsin, pancreatin, and diastase by fifteen different sulfonamides has been investigated.
All sulfonamides tested remove these enzymes from their solution. The degree of adsorption by a given sulfonamide depends upon the amount present and the particle size. In addition there are considerable quantitative differences between various sulfonamides.
The adsorption is observed with both crude and crystalline pepsin and trypsin.
The order of adsorptive capacity seems to be related qualitatively to the pKa values of the different sulfonamides.
The adsorption of pepsin on microcrystalline sulfathiazole apparently causes some irreversible changes because only part of the enzyme activity can be found following separation from the sulfonamide.
Footnotes
- Received November 13, 1950.
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