Abstract
Leucine aminopeptidase (LAP) is a Zn-enzyme localized in the cytosol and occurring in the tissues and body fluids of all organisms. LAP, crystallized at first from bovine eye lens, TM shows a total or partial immunological identity in different tissues of vertebrates (liver, kidney) and also in different vertebrate species. Immunological assay can establish a phylogenetic relationship between LAP from man, cattle, and frog spanning an evolutionary time of about 280 million years. LAP crystallized from bovine eye lens is nearly identical with the enzyme from the cytosol of pig kidney. However, it is clearly different in its substrate specificity and in immunological behavior from particle-bound enzyme (aminopeptidase EC 3.4.11.2) of the pig kidney and the enzyme described by Himmelhoch. This chapter elaborates the procedure for enzyme preparation and crystallization, its key physical and kinetic properties and its purity. It also elaborates on several assay methods to determine the activity of leucine aminopeptidase.
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