Walter Oberthür

Adaptation of hemoglobin function to subterranean life in the mole, talpa europaea

In order to understand the mechanism responsible for the high oxygen affinity of mole blood, we investigated in the mole. Talpa europaea, red cell parameters that determine hemoglobin function. We have found that the oxygen half saturation pressure (P50) of mole blood is 2.85 kPa (21.4 Torr) at pCO2 4.7 kPa, pH 7.4 and 37 degree C. The concentration of 2,3-diphosphoglycerate (2,3-DPG) averaged 5.3 mmol/l in red cells. In addition, we have determined P50 in hemoglobin solutions at various concentrations of 2,3-DPG at an assumed intraerythrocytic pH of 7.2 and 37 degree C. These data were used to calculate the association constants of 2,3-DPG to mole hemoglobin. P50 was 1,89 kPa (14.2 Torr) in hemoglobin solutions without 2,3-DPG. The response to 2,3-DPG was relatively low. Noteworthy, CO2 did not affect the oxygen affinity at constant pH in the presence of 2,3-DPG. Our results suggest that the high blood oxygen affinity of the mole can be attributed to a weak interaction of its hemoglobin with 2,3-DPG.

Interconvertible (ZE)-stereoisomers of a vitamin B6 coenzyme analog derived from pyridoxal 5′-phosphate and rhodanine

Abstract The Knoevenagel condensation product of pyridoxal 5′-phosphate (1) with rhodanine (2) was prepared and identified as (Z)-5-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]-2-thioxo-4-thiazolidinone (3). The labile (E)-stereoisomer 4 was obtained in a crude form. Its association with the nucleobase adenine was prepared suggesting an affinity to nucleic acids.