来自沼泽红假单胞菌的胆色素原酶。
Porphobilinogenase from Rhodopseudomonas palustris.
作者信息
Juknat A A, Kotler M L, Koopmann G E, Batlle A M
机构信息
Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (FCEN, UBA--CONICET), Cjudad Universitaria, Buenos Aires, Argentina.
出版信息
Comp Biochem Physiol B. 1989;92(2):291-5. doi: 10.1016/0305-0491(89)90280-0.
PMID:2924537
Abstract
- Porphobilinogenase (PBGase) from Rp. palustris has been isolated and some properties of a partially purified fraction were studied. 2. PBGase has an optimum pH of 7.4 when activity was expressed in terms of porphyrins formed and two pH maxima at 7.4 and 8.5 when activity was based on the amount of PBG consumed. 3. Cyclotetramerization rate and distribution of reaction products were not affected either by the presence or absence of oxygen. 4. Two PBGase active species of mol. wt 115,000 and 50,000 were found, by means of gel filtration through a calibrated Sephadex G-100 column. 5. Kinetic data show the existence of positive cooperative effects for porphyrin formation, while a hyperbolic behaviour for PBG consumption was observed.
摘要
- 已从沼泽红假单胞菌中分离出胆色素原酶（PBGase），并对部分纯化组分的一些性质进行了研究。2. 以形成的卟啉表示活性时，PBGase的最适pH为7.4；以消耗的PBG量为基础时，在7.4和8.5有两个pH最大值。3. 氧的存在与否均不影响环四聚化速率和反应产物的分布。4. 通过经校准的Sephadex G - 100柱进行凝胶过滤，发现了分子量为115,000和50,000的两种PBGase活性物质。5. 动力学数据表明卟啉形成存在正协同效应，而观察到PBG消耗呈双曲线行为。
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