Eötvös Loránd Tudományegyetem Egyetemi Tanácsának ülései, 1973-1974 (HU-ELTEL 1.a.55-60.)

1974.02.22. rendes - Mellékletek

35} 4 «■ 30./ Keleti, T., Batke, J -: The kinetics of ‘D-glyceraldehyde-3--phosphate oxidation. Acta Physiol,Fung, 28 135 1965 31»/ Boroas, 1«, Keleti, T.; The stability of the ternary complex with ivg of I1' -g}yoaraidébycLe-\3~* jiboaPh_ate d ehydrogenase, Acta PhysiolsHung3 27 397 1965 32./ Keleti, T.; The role of SH-groups in the ctalytic activity and in the atabiliaation of structure of dehydrogenaaea 0 Acta Biol „Med. Germanica, Supplementband III, 245 1965 33. / Keleti, 34. / Keleti, 35-/ Telegdi 36. / Keleti, 37. / Keleti, 38. / Keleti, 39. / Keleti, T.: Data on the D-glyceraldehyde oxidation. Acta PhyaioloHung. 29 101 19&6 T., Telegdi, M.: Systematization, completion and differentiation of enzymic inhibition types. Enzymologia 31 39 1966 M», Keleti, T»s Effect of the non-protein component of glycerophosphate dehydrogenase on enzymic activity. Enzymologia 31. 83 1966 T., Boroas, L,: The effect of Ag ions on the binding of Zn to D-glyceraldehyde-3-phoaphate dehydrogenase. Acta Biochim.BiophySoHung® _1 5 1966 T,: Zn in yea3t D-glyceraldehyde-3-phosphate dehydrogenaseo BiochimoBiophys.Res.Oommuna 22 640 1966 T.: The liberator JcTheoret.Biols 16 337 1967 T., Batke, J.: The pH dependence of apparent Michaelis constants and maximum velocity in D-glyceraldehyde­­-3TMphosphate oxidation. Enzymologia 33 65 1967

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