Evidence for the existence of homologous gene coding regions for the catecholamine biosynthetic enzymes.
Evidence for the existence of homologous gene coding regions for the catecholamine biosynthetic enzymes.
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儿茶酚胺生物合成酶同源基因编码区存在的证据。
DOI：
10.1101/sqb.1983.048.01.036
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发表时间：
1983
期刊：
影响因子：
--
通讯作者：
Reis,DJ
中科院分区：
文献类型：
--
作者：
Joh,TH;Baetge,EE;Ross,ME;Reis,DJ
方法制备抗CA合成酶抗体。纯化CA合成酶TH、DBH和PNMT，并如其他地方所述在兔中产生针对纯化酶的抗体（Joh和Ross 1983）。通过SDS-聚丙烯酰胺凝胶电泳测定每种酶的分子量。TH、DBH和PNMT的分子量分别为60、75和31 kD。已知当TH用胰蛋白酶处理短时间（室温下10-30分钟）时，可以获得较小（35 kD）的物质。这种胰蛋白酶消化形式的TH（tTH）通常比天然形式的TH具有更高的比活性。每种酶（包括tTH）的抗体不与任何其他蛋白质发生交叉反应，但粗品、部分纯化或纯化酶制剂中的自身抗原除外（Joh和Ross 1983）。与其他CA合成酶没有交叉反应性已被证明免疫组化和免疫化学沉淀。
METHODSPurification of and production of antibodies to CA-synthesizing enzymes. CA-synthesizing enzymes, TH, DBH, and PNMT, were purified, and antibodies against purified enzymes were raised in rabbits as described elsewhere (Joh and Ross 1983). The molecular weight of each enzyme was determined by SDS-polyacrylamide gel electrophoresis. Molecular weights of TH, DBH, and PNMT were 60, 75, and 31 kD, respectively. It is known that when TH is treated with trypsin for a short period of time (10-30 min at room temperature), a smaller (35 kD) species can be obtained. This trypsin-digested form of TH (tTH) usually has higher specific activity than the native form of TH. Antibodies to each enzyme, including tTH, do not cross-react with any other protein except their own antigen in crude, partially purified, or purified enzyme preparations (Joh and Ross 1983). No cross-reactivity with other CA-synthesizing enzymes has been demonstrated by immunohistochemistry and immunochemical precipitation.