Characterization of the pyruvate kinase which induces the low 2,3-DPG level of fetal rabbit red cells.

Abstract

The low 2,3-disphosphoglycerate (2,3-DPG) level of fetal rabbit red cells has been attributed previously to a very high pyruvate kinase (PK) activity. The present report shows that the high PK activity is associated with a distinct fetal isozyme. Fetal and adult rabbit red cell PK were characterized by the methods recommended by the International Committee for Standardization in Haematology. Fetal red cell PK differed from the adult enzyme by its greater thermostability, lower affinities for phosphoenolpyruvate and ADP, higher nucleotide specificity and lower ATP inhibition. Marked electrophoretic differences were not detected. Our results indicate that there is a developmental change in red cell PK isozyme expression in the rabbit. We do not know, however, if this change arises at the gene level or from cell-age dependent postsynthetic modifications of the enzyme. But in view of the role of PK in the control of the 2,3-DPG level and thereby of the oxygen affinity of red blood cells, we assume that the physiological significance of the PK isozyme change is akin to that of the switch from fetal to adult hemoglobin in other species.