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- W2024852923 abstract "Summary Histaminase or diamine: oxygen oxydoreductase (E.C.1.4.3.6.) has been purified 9,600 times from human placenta. The major difficulty was to eliminate hemoglobin from the extracts. In addition, the enzyme has to be stabilized by sucrose during the last steps. As fractionation progresses, a latency time up to 3 h 30 mn modifies the enzymatic kinetic. This latency time is annihilated by preincubation without histamine at 37°C. The enzyme requires Mn++ ions and hemoglobin; there is a potentiating effect for these activators. The isoelectric point is near 6.0 and histaminase is unstable at this pH. The optimum pH is 7.4. The optimum temperature is superior to 45°C. Filtration on Biogel reveals 4 active forms whose molecular masses are multiples from 1 to 4 of 125,000 ± 5,000. Apparent Michaelis constants determined for histamine, putrescine and cadaverine are respectively 0.6 × 10−5 M, 3.3 × 10−6 M and 3.3 × 10−6 M. Histaminase is inhibited by excess histamine but other diamines do not entail this result. Monoamines are not altered by the enzyme. Aminoguanidine is the best inhibitor; semicarbazide is much less active. According to several of its physico-chemical characteristics, diamine: oxygen oxydoreductase from human placenta is different from similar enzymes already described." @default.
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- W2024852923 date "1971-01-01" @default.
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- W2024852923 title "Purification et propriétés de la diamine: oxygène oxydo-reductase du placenta humain" @default.
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- W2024852923 doi "https://doi.org/10.1016/s0300-9084(71)80114-1" @default.
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