Effect of binding to hemoglobin and albumin on pyridoxal transport and metabolism.
Scatchard plot analysis indicated that pyridoxal binds to hemoglobin more than twice as tightly as it does to serum albumin. Comparison of the formation constants for hemoglobin and albumin, using standard competitive binding equations, indicated that the distribution ratio for pyridoxal between erythrocytes and plasma should be 6.5:1. This distribution was approximately the same as that observed when pyridoxal was incubated with whole human blood, suggesting that these two proteins are the primary determinants of the pyridoxal distribution in whole blood. With in situ perfused rat liver the uptake of [3H] pyridoxal from the perfusate was reduced by the inclusion of erythrocytes in the perfusate. This was reflected in the decreased production of 4-pyridoxic acid by the perfused liver from 3.8% to 1.2% of the dose by the addition of erythrocytes to the perfusate. The major labeled metabolites found in the liver were pyridoxal phosphate, pyridoxamine phosphate, and 4-pyridoxic acid for both types of perfusion. In intact animals, reduction of the erythrocytes concentrations to hematocrits of 30-40% increased the recovery in the urine of 3H from administered [3H] pyridoxal from control values of 27-35% to 40-50% of the dose within 48 h. Half of the label in urinary metabolites was in 4-pyridoxic acid.
D000818:Animals; D001667:Binding, Competitive; D004912:Erythrocytes / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008297:Male; D011485:Protein Binding; D011730:Pyridoxal / Q000031:analogs & derivatives / Q000097:blood*; D051381:Rats; D011919:Rats, Inbred Strains; D012709:Serum Albumin / Q000378:metabolism*; D013329:Structure-Activity Relationship
D006454:Hemoglobins; D012709:Serum Albumin; D011730:Pyridoxal