Observations on a Case of Partial De - Ficiency of Erythhocytic Atpase

S 489 phy. From the Dept. of Medicine, University Hospitals, Cleveland, Ohio. J. Clin. Invest., 47:1483-1495, 1968. Suspensions of erythrocytes from patients with Hb CC disease showed an increased viscosity and decreased filterability suggesting a less deformable cell. Hemolysates prepared from Hb CC erythrocytes had an increased viscosity compared with hemolysates of normal cells, suggesting that the increased viscosity of Hb CC cells in serum was the result of an increased internal viscosity of the cell. These abnormal rheobogical properties of Hb CC erythrocytes were associated with a decreased content of cations and an abnormality of cell water. The fraction of the cell volume which is water in Hb CC cells was 95.5% of normal. The amount of cell water in Hb CC cells available for osmotic equilibrium, termed solvent water, was only 67 % of that in normal cells. The smaller amount of solvent water in Hb CC cells indicates a greater amount of water bound to protein.-T. N. BETA THALASSEMIA TRAIT: DETECTION AT BIRTH. Y. W. Kan and D. C. Nathan. From the Hematology Research Laboratory, Children’s Hospital Medical Center, Boston, Mass. Science, 161:589-590, 1968. The authors were able to detect, on the basis of in vitro incorporation of C’4-leucine into and /3 chains of cord blood, the presence of fi-thalassemia trait in the newborn. Abstracter’s comment: This represents the second, and possibly more sensitive, method of diagnosing thalassemia in the newborn. Unfortunately, the authors have not as yet had the opportunity to study a patient with homozygous thalassemia.-T. N. EVIDENCE FOR MULTIPLE STRUCTURAL GENES FOR THE y CHAIN OF HUMAN FETAL HEMOGLOBIN. W. A. Schroeder, T. H. J. Huisnian, J. R. Shelton, J. B. Shelton, E. F. Kleihaver, A. M. Dozy, and B. Robberson. From the Div. of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, Cal. Proc. Nat. Acad. Sci. (U.S.A.), 60:537544, 1968. Human fetal Hb in the normal infant at birth is composed of at least 2 components that are not separable by column chromatography or electrophoresis. At a minimum, they differ in the exchange of glycine and alanine in position 136 of the y chain. On the basis of evidence from abnormal human fetal hemoglobins, it is concluded that these types of y chains are the products of more than one structural gene and are not the results of ambiguity of translation of the genetic material. The quantitative relationships that have been observed are not easily explained on the basis of current concepts on the control of protein synthesis. Abstracter’s comment: A very important paper in that it may explain many of the findings in patients with persistent elevations of fetal hemoglobin.-T. N.