人血浆高分子量组分对单胺氧化酶的激活作用。
Activation of monoamine oxidase by high molecular weight fractions of human plasma.
作者信息
Wahlund L O, Sääf J, Ross S B, Wetterberg L
出版信息
Acta Physiol Scand. 1984 Mar;120(3):337-41. doi: 10.1111/j.1748-1716.1984.tb07393.x.
The activation of human platelet monoamine oxidase (MAO) and rat brain mitochondrial MAO ( RBM -MAO) by human plasma were studied. The deamination of two different substrates, tyramine and phenethylamine (PEA) was investigated. The increase in MAO activity in the presence of human plasma can be explained by the observed decrease in the apparent Km for the amine (tyramine, PEA). This activation pattern was the same both for human platelet MAO and RBM -MAO. The activating properties of human plasma were recovered in high molecular weight fractions after gel filtration.
研究了人血浆对人血小板单胺氧化酶（MAO）和大鼠脑线粒体MAO（RBM-MAO）的激活作用。考察了两种不同底物酪胺和苯乙胺（PEA）的脱氨基作用。人血浆存在时MAO活性的增加可以通过观察到的胺（酪胺、PEA）表观Km值的降低来解释。这种激活模式在人血小板MAO和RBM-MAO中是相同的。凝胶过滤后，人血浆的激活特性在高分子量组分中得以恢复。
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