ALBERT

Description: Postnatal synthesis of fetal and adult hemoglobin was studied with radioactive iron (Fe59) and glycine-2-C14 in newborn goats. At birth about 60 per cent of Hb-F is present in newborn goats; after 60 days only about 5 per cent is found. Two goats were treated with "exchange transfusions" with blood of the mother. Using an alkali denaturation method the fetal hemoglobin was not demonstrable during the first few days after this treatment, but 20 days later about 20 per cent was present in circulating blood. Maxima of radioiron-specific activity in adult hemoglobin occurred in untreated newborn goats at the 12th day, of C14 at the sixth day; in "exchange goats" for radioiron at the 8th day. The fetal hemoglobin maxima of specific activity occurred in the untreated goats resp. after 32 and 24 days, in "exchange goats" after 8 days. The reappearance of Hb-F in "exchange goats" and the specific activity of Hb-F are direct indications for a synthesis of this component after birth in this species.

Description: This study illustrates that the value of both alkali denaturation methods is somewhat limited. At high percentages of fetal hemoglobin, the results obtained with the method of Singer and coworkers, are about 10 per cent too low. The Brinkman and Jonxis method is not accurate when the percentage of fetal hemoglobin is lower than 10 per cent. The alkali resistant fraction found with the method of Singer and associates in adult blood, is a mixture containing fetal hemoglobin. The presence of COHb-A will interfere with the determination of fetal hemoglobin, especially when the optional alkali denaturation method is used.

Description: 1. The present paper describes an apparently white family in which a few members suffered from homozygous and heterozygous hemoglobin C disease. Since the paternal great grandfather and the maternal grandfather of the patients examined were in a family relation of the first order, it is surmised that the hemoglobin C was derived from the same homozygous negroid (?) ancestor. Besides its occurrence in this family Hb-C is also found in a colored family from the same island (Curaçao). 2. Hemoglobin C shows, in addition to abnormal electrophoretic mobility, three other more or less specific properties: a. During chromatographic examination carried out with the aid of the cation exchanger Amberlite IRC 50 (XE 64), a citrate citric acid buffer at pH 6 and sodium ion concentration of 0.15, COHb-C displaces itself noticeably slower than the three other forms of hemoglobins (S, A and F). b. The solubility of the COHb-C in a phosphate buffer pH 6.5 of various concentrations is significantly less than that of COHb-S, COHb-A and COHb-F. The reduced form of hemoglobin C does not show this property; the solubility of this is practically the same as that of reduced adult hemoglobin. c. A comparison of the amino acid composition of hemoglobin C and hemoglobin A, S and F, shows that COHb-C contains a higher number of lysine and perhaps histidine residues. This increase amounts to four residues per mol. for lysine and one residue per mol. for histidine. The possible connection between the more basic character of the proteins and the abnormal behavior in the electrophoretic and chromatographic experiments is discussed. 3. The results obtained with five experimental methods (electrophoresis, alkali denaturation, chromatography, salting-out experiments, and amino acid composition determination) all seem to indicate that in the homozygous form of this disease only the abnormal Hb-C is present. None of the other three hemoglobins (A, S and F) were shown to be present in determinable amounts. 4. In addition to the electrophoretic abnormalities, the above three properties may be of importance in the characterization of this abnormal hemoglobin.