[Physiological importance of microvilli-bound leucine arylamidase in the final digestion of proteins. 1. Purification and isolation of intestinal leucine arylamidase and aminotripeptidase of rats].

The membrane-bound leucine arylamidase of the microvilli of the rat small intestine was solubilized by Triton X-100 and purified by gel and ion-exchange chromatography. As compared to the mucosa homogenate, the purification factor was 135. The leucine arylamidase and aminotripeptidase of the microvilli cannot be separated by chromatography. The cytosomal portion of the aminopeptidase is devoid of leucine arylamidase activity.