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- W2015121406 abstract "Human pancreas is the source of an alanine aminopeptidase (HPAA) that is unique to pancreas and is readily distinguishable from the liver, kidney, and duodenal alanine aminopeptidases. Each of these three aminopeptidases appears in small quantities in blood and therefore may constitute tissue/organ specific marker enzymes. In this study alanine aminopeptidase from pancreas has been purified. Pancreas alanine aminopeptidase was resolved upon purification with ion exchange chromatography into three isoenzymes. Gel filtration chromatography of these isoenzymes indicates that their molecular weights are near 235 000 daltons. The isoenzymes contain a firmly bound divalent cation that could be removed with EDTA only at temperatures above 40°C (at which the enzymes were stable) and below 52°C (at which thermal denaturation begins to take place). Treatment with EDTA at 4°C yields fully active enzymes, which, however may be stimulated approximately 200% by the addition of Co 2+ at 10 −4 mol/1. This cobalt stimulation is easily reversed by dialysis of the stimulated isoenzymes against deionized water. The pancreas alanine aminopeptidases were not inhibited by tosyl-phenylalanine chloromethylketone or by tosylleucine chloromethylketone, whereas phenylalanine chloromethylketone was inhibitory. The K m values for methionyl-, arginyl-, leucyl-, alanyl-, and isoleucylβ-naphthylamide for each isoenzyme are statistically identical and the average values are 0.36, 0.60, 0.69, 1.25, and 1.29 × 10 −4 mol/1, respectively. The k cat values are 2.50, 1.58, 0.82, 0.38, and 0.19 × 10 4 sec −1 , respectively." @default.
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- W2015121406 date "1980-06-01" @default.
- W2015121406 modified "2023-09-27" @default.
- W2015121406 title "Multiple molecular forms of human pancreas alanine aminopeptidase" @default.
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- W2015121406 doi "https://doi.org/10.1016/0009-8981(80)90193-x" @default.
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