Kinetic behaviour and oligomeric state of 3-phosphoglyceroyl-D-glyceraldehyde-3-phosphate dehydrogenase
1981; Elsevier BV; Volume: 63; Issue: 2 Linguagem: Inglês
10.1016/s0300-9084(81)80170-8
ISSN1638-6183
AutoresMária Vas, Susan Lakatos, János Hajdu, P. Friedrich,
Tópico(s)Metabolism and Genetic Disorders
ResumoThe specific activity of pig muscle d-glyceraldehyde-3-phosphate dehydrogenase was found to be constant in the reverse reaction, with NADH and 1,3-diphosphoglycerate as substrates, over the enzyme concentration range 10-8 to 10-4 M. The molecular weight of the covalent intermediate of the enzyme, 3-phosphoglyceroyl-glyceraldehyde-3-phosphate dehydrogenase, as measured by sedimentation techniques, proved constant (145 000 ± 6 000) between 3 × 10-7 and 3 × 10-5 M enzyme concentration. Likewise, no change in the apparent molecular weight was observed by gelcentration. The data indicate that the enzyme functions in its tetrameric form.
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