[41] Human liver aminopeptidase

摘要: Publisher Summary Human liver aminopeptidase (HLA) catalyzes the hydrolysis of N-terminal amino acid residues from peptides, aeid amides, or certain ehromogenie synthetic substrates. The rate is maximum when residue L-alanine, but other acids with nonpolar R groups, for example, L-leueine, are hydrolyzed at significant rates. Since one first commonly available synthetie substrates aminopeptidases was L-leueyl-fl-naphthylamide, it initially assumed by many investigators that HLA aetivity could be attributed to leueine (LAP), now clear chemically distinct LAP. must assayed a variety and under conditions, depending on state purity enzyme specific results desired. This chapter details various applicable assay methods necessary detailed work this enzyme. These based, first, substrate used, then instrumental available. following have been discussed in chapter: Assay Aminoacyl-fl-naphthylamide Substrates (Colorimetric Method, Fluorometric Spectrophotometric Method), Aminoacyl-p-nitroanilide ( Method) Dipeptide Amino Acid Amide (Spectrophotometric method, Colorimetric Ninhydrin Method). It also discusses Purification Liver Aminopeptidase.