Immunocytochemical Localization of Lysosomal Cysteine and Aspartic Proteinases, and Ubiquitin in Rat Epidermis.

Immunocytochemical localization of lysosomal cysteine and aspartic proteinases, and ubiquitin in rat epidermis.

To analyze the degradation system in epidermal cells during their generation, differentiation, and cell death, immunocytochemical localization of lysosomal cysteine and aspartic proteinases, an endogenous cysteine proteinase inhibitor, cystatin beta, and ubiquitin were examined using rat sole skin. By confocal laser microscopy, granular immunodeposits for lysosomal proteinases were well demonst...

Lysosomal Cysteine and Aspartic Proteases

Immunocytochemical localization of lysosomal beta-galactosidase in rat liver

beta-galactosidase is a ubiquitous lysosomal hydrolase that specifically cleaves terminal beta-galactosyl residues from glycoproteins, glycosaminoglycans, oligosaccharides, and glycolipids. To study the intracellular distribution of this enzyme, we prepared a specific polyclonal antibody to lysosomal beta-galactosidase by immunizing rabbits with a highly purified preparation of beta-galactosida...

Aspartic proteinases and their inhibitors.

Proteolytic enzymes are classified on the basis of their catalytic mechanism as belonging to one of four groups: the serine, cysteine, metallo and aspartic proteinases (Kay, 1982). In contrast to the detailed sequence information and three-dimensional structures that have been produced for many enzymes belonging to the first three groups, relatively little is known about the aspartic proteinase...

Structure and function of plant aspartic proteinases.

Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues indispensible for catalytic activity. The three-dimensional structure of two plant aspartic proteinases has been determined, sharing significant structural...