HISTOCHEMICAL STUDIES OF AMINOPEPTIDASE BY MEANS OF L-N(5-BROMOINDOL-3- YL)LEUCINAMIDE
Abstract
Aminopeptidase in tissue and component cells thereof can be demonstrated by a new synthetic indolyl substrate with leucine attached to a halogen-substituted indolyl moiety. The tissue enzyme hydrolyzes the peptide bond adjacent to the free amino group to form a chromogenic bisindigo at enzymic sites within the cells and tissues. Evidence of high enzyme activity was seen in the kidney, parathyroid gland, and connective tissue cells of the lamina propria. The enzyme activity in the kidney was most intense in the lower cortex; the activity of the upper cortex was about one-half. In the upper cortex, the enzyme was present mainly in the basilar region of the cell, whereas, in the lower cortex, it was more intense in the luminal portion. The medulla of the kidney showed only a slight reaction. Conspicuous and high enzyme activity was seen in certain connective tissue cells of the lamina propria. These cells tend to exhibit certain fibrillary processes. The stroma of the endometrium of the uterus revealed cells with high activity. These cells have an elongated cytoplasm with a dense nucleus and are morphologically similar to other stromal cells in the proliferative stage of the endometrium. The parathyroid gland showed a strong enzyme reaction that was uniformly distributed throughout the cells of the gland. The thyroid gland showed a medium enzyme activity, seen as granules in the follicular epithelial cells. The liver showed a medium activity. The thymus showed activity mainly in the reticuloendothelial cells. There was a great deal of variation in enzyme activity that seemed to depend upon physiological states. Thus, in the ovary, there was marked activity in the atretic follicle.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 1968
- Accession Number
- AD0835830
Entities
People
- Bjarne Pearson
- William E. Bennett