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- W72135613 abstract "Publisher Summary Meprin, the name is an acronym for metallo-endopeptidase from renal tissue, is an intrinsic plasma membrane proteinase. The enzyme was discovered as the activity in mouse kidney homogenates that was responsible for the high rate of degradation of the general proteinase substrate, azocasein. Meprin was purified, was named, some of its properties were characterized, and its subcellular localization was determined in the laboratories. An inherited deficiency of meprin activity was subsequently discovered in some inbred mouse strains, a rare if not unique example of a heritable deficiency of a cellular proteinase. In addition, the gene that controls meprin activity has been located on chromosome 17 near the major histocompatibility complex. Proteases, endopeptidases and exopeptidases, have been the focus of numerous scientific studies. Indeed purified proteolytic enzymes have provided the material for many investigations of the fine structure of enzymes, the physicochemical interactions between macromolecules or between macromolecules and small ligands, and the chemical kinetics of enzymes." @default.
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- W72135613 date "1986-01-01" @default.
- W72135613 modified "2023-09-25" @default.
- W72135613 title "Meprin: A Membrane-Bound Metallo-endopeptidase" @default.
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- W72135613 doi "https://doi.org/10.1016/b978-0-12-152828-7.50009-3" @default.
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