Mouse mammary carcinoma porphobilinogenase and hydroxymethylbilane synthetase
1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM...
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1991
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v98_n1_p67_Navone http://hdl.handle.net/20.500.12110/paper_03050491_v98_n1_p67_Navone |
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| Sumario: | 1. 1. Porphobilinogenase (PBGase) and hydroxymethylbilane synthetase (HMB-S) were investigated in crude extracts from mouse mammary carcinoma, normal mouse liver and tumor bearing mouse liver. 2. 2. A Michaelis-Menten kinetics for both enzymes in either source was observed. Km values of 87 to 108 μM, Vmax of 1.57-1.83 nmol porphyrins/2 hr and a Hill coefficient of n = 1 were obtained for PBGase and Km values of 13 to 19 μM and Vmax of 2.6-4.8 were obtained for HMB-S. 3. 3. Porphyrin synthesis was linear up to 180 min of incubation in all cases for PBGase and HMB-S, and greatly increased with higher incubation temperature being maximal at 60°C and nil at 70°C, optimal temperature was 37°C for either enzyme in either source. 4. 4. Uroporphyrinogen III synthetase was heat inactivated while HMB-S was a heat stable enzyme. Optimum pH was 8.2 for PBGase and HMB-S in either tissue. © 1991. |
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