Autoxidation of extracellular oxyhaemoglobin from the polychaete Perinereis brevicirris (Grube)
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Abstract 1. 1. SDS-polyacrylamide gel electrophoresis showed that the Perineis haemoglobin consisted of three subunits with mol. wt of 12,000 (subunit 1), 40,000 (subunit 2) and 54,000 (subunit 3) in a molar ratio of 1:4:3. 2. 2. At alkaline pH, the oxyhaemoglobin dissociates into subunits. Therefore, the two haem-containing, subunits 1 and 2, could be separated by gel filtration on a Sephadex G-75 column. 3. 3. The autoxidation rates of oxyhaemoglobin and the oxy-forms of the haem-containing subunits to met-forms were measured in the pH range of 5.4–11.6 and the pH dependencies of their autoxidation rates were compared with that of vertebrate oxymyoglobin. 4. 4. The autoxidation rates of subunits 1 and 2 were approx 500 and 30 times, respectively, that of the intact haemoglobin at pH 7.5. 5. 5. The activation energy of the autoxidation reaction of the whole oxyhaemoglobin was calculated to be 30.5 kcal/mol at pH 7.2.
収録刊行物
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- Comparative Biochemistry and Physiology Part B: Comparative Biochemistry
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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 75 17-21, 1983-01-01
Elsevier BV