Porphobilinogenase from Rhodopseudomonas palustris |
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| Authors: | A A Juknat M L Kotler G E Koopmann A M Batlle |
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| Affiliation: | Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (FCEN, UBA--CONICET), Cjudad Universitaria, Buenos Aires, Argentina. |
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| Abstract: | 1. 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. |
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