STUDIES ON THE FATE OF PLASMA PROTHROMBIN

The level of the plasma prothrombin in the circulating blood is decreased during its passage through the pulmonary capillaries. In 85 per cent. of samples, plasma prothrombin has been found to be less in the blood of the left ventricle than in that from the right ventricle. This difference averaged 10.6 per cent. and ranged from 4 to 19 per cent. In no instance was the level in the right ventricle lower than that in the left. In samples of blood taken from the arterial and venous supply of the head, liver, spleen, intestine, kidney and hind limbs, no significant difference in plasma prothrombin levels was found. A possible explanation of this role of the lung in the loss of plasma prothrombin is thought to be the production of blood platelets in this organ, as demonstrated by Howell and Donahue. Platelets, as they undergo disintegration, initiate the first stage of the clotting process by releasing thromboplastin, which, in the presence of calcium, changes prothrombin to thrombin.     

Racemization of Amino Acids in Dipeptides Shows COOH > NH2 for Non-Sterically Hindered Residues

The relative rates of racemization for amino acid residues at the NH(2) and COOH ends of 37 different dipeptides were determined. In nine dipeptides containing alanine, leucine, phenylalanine, aspartic acid, and methionine, the amino acid residue racemized faster at the COOH-terminal position than at the NH(2)-terminal position (COOH > NH(2)). The sterically hindered amino acids isoleucine and valine showed NH(2) > COOH. Six proline dipeptides showed NH(2) > COOH. Intramolecular effects have been invoked to explain these surprising results.