Influences of proteolytic enzymes on parotin. IV. Separation of hydrolyzates in digested parotin by trypsin. (Studies on the physiological chemistry of the salivary glands. LII).

Abstract

The hydrolyzates in the digested parotin by trypsin were separated into the 3 fractions by the isoelectric precipitation and acetone fractionation: the pH 4.5-precipitate, the insoluble fraction in the acetone of 80% concentration, and the soluble fraction in the same solvent. The first pH 4.5-precipitate was relatively pure in view of the paper electrophoresis and the paper partition chromatography, and showed the same biological activities as the parotin before digestion. The 80% acetone-insoluble fraction was the mixture of some hydrolyzates and showed only the leukocyte increasing activity. The 80% acetone-soluble fraction contained many hydrolyzates and was negative in the biological activities.