Characterization and purification of polymorphic arylalkylamine N-acetyltransferase from the American cockroach, Periplaneta americana
Characterization and purification of polymorphic arylalkylamine N-acetyltransferase from the American cockroach, Periplaneta americana
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DOI：
10.1016/s0965-1748(01)00075-3
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发表时间：
2001-12-01
影响因子：
3.8
通讯作者：
Takeda, M
中科院分区：
文献类型：
--
作者：
Ichihara, N;Okada, M;Takeda, M
我们从美洲大蠊（Periplaneta americana）的不同器官中分离出两种形式的芳烷基胺N-乙酰转移酶（AANAT）。两种形式的酶具有28 kDa的等效分子量。从睾丸副腺分离的一种形式在酸性pH下具有高酶活性。其等电点为5-6，底物特异性较其它类型广。从女性中肠的其他分离形式有较高水平的酶活性在碱性pH值。这些发现表明，美洲果蝇含有多态性AANAT，就像果蝇一样。这些形式不仅在pH特异性上不同。和底物特异性，但在色谱行为和动力学性质。我们检查的大多数器官含有两种形式的混合物，因为当两种pH条件用于活性测量时，两种类型的AANAT活性在不同的色谱级分中分离。(C)2001年由Elsevier Science Ltd.出版
We separated two forms of arylalkylamine N-acetyltransferase (AANAT) from various organs of the American cockroach, Periplaneta americana. Both forms of the enzyme had an equivalent molecular mass of 28 kDa. One form isolated from the testicular accessory glands had high enzyme activity at acidic pHs. The isoelectric point was 5-6 and the substrate specificity was wider than the other type. The other isolated form from female midguts had a higher level of enzyme activity at basic pHs. These findings suggested that P. americana contains polymorphic AANAT, as is the case in Drosophila melanogaster. These forms differed not only in pH specificity. and substrate specificity but in chromatographic behavior and kinetic properties. Most of the organs we examined contained a mixture of the two forms since two types of AANAT activity were separated in different chromatographic fractions when two pH conditions were used for activity measurement. (C) 2001 Published by Elsevier Science Ltd.