Isolation and Characterization of Human Gastric Procathepsin E and Cathepsin E
Human gastric cathepsin E is an aspartic proteinase present in human gastric mucosa and different from pepsinogens A and C and cathepsin D. It has been localized not only to stomach mucosa, but also to erythrocyte membranes and several lymphoid associated tissues and cells including thymus, spleen, macrophages and polymorphonuclear lymphocytes (1,2). However its physiological function and the process of activation remain obscure. Due to its intracellular localization in lymphoid associated tissues and cells it has been suggested to have a role in immune function (3,4). Studies on cathepsin E has not progressed like those on other aspartic proteinases (pepsinogens and cathepsin D), because of difficulties in obtaining a sufficient amount of the purified native enzyme. Therefore, to understand the structure-function relationship of cathepsin E and to clarify its physiological function, it is important to establish a purification procedure of procathepsin E and cathepsin E for further characterization.
KeywordsCellulose Hydrolysis High Performance Liquid Chromatography Fluoride Lysin
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