The presence in certain pathological urines of protein-like material which is not coagulated by heat has been realized for some years. It has been called mucin, mucoid, nucleoprotein, phosphoprotein, mucoprotein and nucleoalbumin by different investigators and has usually been detected by the turbidity produced on rendering the diluted urine acid with acetic acid. The isolation and characterization of a similar substance in normal urine was first reported by Tamm & Horsfall (1950, 1952), who employed two methods of isolation, one relying on ethanol precipitation and the other on saltingout with 0-58M sodium chloride. Yields in both cases were of the order of 2-2-5 mg./100 ml. of urine. Data on this substance suggest that the term 'mucoprotein' is appropriate (Tamm &

With data on 91 alloimmunized thrombocytopenic patients and 389 donor- recipient pairs matched or selectively mismatched for HLA antigens, it was observed that ABO incompatibility significantly reduced the effectiveness of platelet transfusions. The mean 24-hr recovery of platelets from histocompatible donors and from donors selectively mismatched for cross-reactive HLA antigens was decreased by approximately 23% if the donor typed for blood group A and/or B not found in the recipient. Thus, the reduction in platelet recovery associated with ABO incompatibility is not of a magnitude that would contraindicate transfusion of ABO-mismatched platelets.

The structure and bonding properties of metal complexes in subcritical and supercritical fluids are still largely unknown. Conventional high pressure and temperature cell designs impose considerable limitations on the pressure, temperature, and concentration of metal salts required for measurements on solutions under supercritical conditions. In this study, we demonstrate the first application of the diamond anvil cell, specially designed for x-ray absorption studies of fn'st-row transition metal ions in supercritical fluids. Zn K-edge XAFS spectra were measured from aqueous solutions of 1-2m ZnC12 and up to 6m NaC1, at temperatures ranging from 25-660 °C and pressures up to 800 MPa. Our results indicate that the ZnC142-complex is predominant in the lm ZnC12/6m NaC1 solution, while ZnC12(H20)2 is similarly predominant in the 2m ZnC12 solution, at all temperatures and pressures. The Zn-C1 bond length of both types of chlorozinc(II) complexes was found to decrease at a rate of about 0.01 A/100 °C.

No abstract

581purification experiments were severely hampered by the lability of the enzyme.2. Peptide-bond formation specifically required adenosine triphosphate, and magnesium ions could be replaced to a considerable extent by manganous ions. Carnosine synthesis was not readily reversible. Pyrophosphate was strongly inhibitory, and orthophosphate less so. Although the enzyme preparation promoted [32P]pyrophosphate incorporation into adenosine triphosphate, a dependency upon ,-alanine could not be clearly demonstrated.In fact, this process was suppressed by a high Palanine concentration. Fluoride ions inhibited both carnosine synthesis and pyrophosphate-adenosine triphosphate exchange.3. Attempts to detect an activated intermediate stage in carnosine synthesis were not successful. 4. g-Alanyl transfer from carnosine to 1-methylhistidine to yield anserine proceeded very slowly, as compared with direct dipeptide synthesis by the enzyme.