Human Hemoglobin Solutions Research Articles

Studies on Hemoglobin: II. The Effect of Anti-Hemoglobin Sera on the Red Blood Cells in Vitro and in Vivo

AbstractImmune sera produced against adult human, fetal, canine and rabbit hemoglobin solutions were found to agglutinate specifically the papain-treated red cells of the respective donors to a high titer. Intact red cells were also specifically agglutinated by the same antibody-containing sera in the presence of dextran, suggesting that the antibodies produced are incomplete ones.A marked shortening of the life span of rabbit erythrocytes followed the intravenous injection of anti-rabbit hemoglobin serum into normal rabbits.The possible implications of the above findings in human pathology are discussed.

Two-dimensional paper-agar electrophoresis of haemoglobin

A two-dimensional electrophoretic technique has been described, based on the different mobilities of haemoglobin on paper at alkaline pH and on agar at acid pH. The method is very sensitive for the detection of small or minute amounts of haemoglobin A in the presence of large amounts of haemoglobin F, and for the detection and closer characterization of other minor components of human haemoglobin solutions.

Starch Block Electrophoretic Studies of Human Hemoglobin Solutions I. Technic and Results in the Normal Adult

Abstract 1. Erythrocyte hemolysates from hematologically normal, adult individuals were studied by means of starch block electrophoresis. 2. The electrophoretic patterns obtained indicated the presence, in addition to the main component of A hemoglobin A1, of three other hemoglobin fractions designated as A2, A3 and A4, A2 and A4 move slower, while A3 moves faster in alkaline buffer. These components were isolated by elution from the starch after separation by electrophoresis. 3. The concentrations of the various fractions in the hemolysates were estimated from a sample of normal individuals investigated. 4. In our experiments, electrophoretic patterns obtained on starch that has been re-used as a supportive medium for electrophoresis were somewhat different but comparable to those obtained on starch that was used for the first time as a supportive medium; these differences are discussed. 5. Some characterizations of the isolated components are made.

Starch Block Electrophoretic Studies of Human Hemoglobin Solutions II. Results in Cord Blood, Thalassemia and other Hematologic Disorders: Comparison with Tiselius Electrophoresis

Abstract The results of starch block electrophoresis of normal adult hemoglobin in the various disease states has been reported. The slow-moving fraction, A2, is elevated in all patients so far studied with thalassemia. Some patients with Addisonian pernicious anemia also show an increase in this fraction. Cord blood contains very little A2. The A2 fraction has no correlation with the severity of the disease. The A2 fraction found on starch seems to be identical with the small, fast-moving component noted in the Tiselius apparatus at acid pH. Iron deficiency anemia of the acquired type tends to have a lower amount of A2 than normal, with an increase to average normal values after therapy.

Abnormal haemoglobins in monkeys.

WE wish to report the finding of abnormal haemoglobins in two species of monkeys. The monkeys had been shot in the Uganda Protectorate as part of another investigation and their blood has been subject to paper strip electrophoresis. At first lysed whole blood was used, but later larger specimens were collected and haemoglobin solutions prepared. Haemoglobins which behaved on electrophoresis like human AA haemoglobin solutions were taken as the normal reference point.

The effect of formaldehyde on the oxygen equilibrium of hemoglobin.

1. When formaldehyde (0.10 M) is added to solutions of human hemoglobin, the oxygen affinity of the hemoglobin increases considerably (more than tenfold near pH 7). The interaction between hemes of the same hemoglobin molecule decreases, as shown by a drop in the value of n in Hill's equation from 2.9 to 1.5 or less. 2. In the presence of formaldehyde, both n and the oxygen pressure for half-saturation fall gradually as the pH rises in the range from pH 6.2 to 7.2. 3. Some of the effect of formaldehyde on the oxygen equilibrium may be due to combination with sulfhydryl groups of the protein, but nitrogenous groups are probably also involved.

Hemoglobin spacing in erythrocytes

Summary 1. The gyration radius of hemoglobin in human erythrocytes was found to be 20–21 A. for normal cells and for cells subjected to osmotic swelling and shrinkage. 2. The low-angle scattering diagrams for normal, swollen, and shrunken human erythrocytes all showed a single diffraction ring; the scattering angle of the ring found for normal cells in isotonic saline corresponded to a value of 64 A. for the quotient λ/sin . 3. The quotient λ/sinvaried in a regular manner with the volume of the red cell. 4. The relationship between the distance λ/sinand the volume per red cell is consistent with the postulate that for normal or shrunken cells the intracellular hemoglobin exists in random orientation and random position except for noninterpenetrability. 5. This isotropic model for shrunken cells is in agreement with results obtained from solutions of human hemoglobin of comparable concentrations, although according to Riley and Herbert (17), the most concentrated solutions show a second diffraction ring which was not observed in our measurements on intracellular hemoglobin. 6. For swollen erythrocytes the values of λ/sinincrease with the cell volume more rapidly than would be predicted for simple isotropic expansion of a system in which the distance between neighboring molecules is related to λ/sinby a constant multiplicative factor k.