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Porphobilinogenase from Rhodopseudomonas palustris.

Authors :
Juknat AA
Kotler ML
Koopmann GE
Batlle AM
Source :
Comparative biochemistry and physiology. B, Comparative biochemistry [Comp Biochem Physiol B] 1989; Vol. 92 (2), pp. 291-5.
Publication Year :
1989

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.

Details

Language :
English
ISSN :
0305-0491
Volume :
92
Issue :
2
Database :
MEDLINE
Journal :
Comparative biochemistry and physiology. B, Comparative biochemistry
Publication Type :
Academic Journal
Accession number :
2924537
Full Text :
https://doi.org/10.1016/0305-0491(89)90280-0