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Observations on the Minor Basic Hemoglobin Component in the Blood of Normal Individuals and Patients with Thalassemia

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Observations on the Minor Basic Hemoglobin Component in the Blood of Normal Individuals and Patients with Thalassemia Observations on the Minor Basic Hemoglobin Component in the Blood of Normal Individuals and Patients with Thalassemia H. G. Kunkel, … , U. Müller-Eberhard, J. Wolf J Clin Invest. 1957;36(11):1615-1625. https://doi.org/10.1172/JCI103561. Research Article Find the latest version: https://jci.me/103561/pdf OBSERVATIONS ON THE MINOR BASIC HEMOGLOBIN COMPONENT IN THE BLOOD OF NORMAL INDIVIDUALS AND PATIENTS WITH THALASSEMIA BY H. G. KUNKEL, R. CEPPELLINI, U. MULLER-EBERHARD, AND J. WOLF (From the Rockefeller Institute for Medical Research, and Institute for the Study of Human Variation, and the Departmet of Pediatrics, Colunma Uniewsity, N. Y.) (Submitted for publication March 6, 1957; accepted April 11, 1957) In a previous report (1) a second hemoglobin was collected from a number of New York hospitals. was described which was found at a concentration The specimens from patients with thalassemia were ob- of tained from Italian and Greek individuals in the hema- approximately 3 per cent in the blood of normal tology clinic at the Babies Hospital, Columbia-Presby- adult individuals. It was found to resemble he- terian Medical Center, New York. Five individuals with moglobin E in electrophoretic properties, but iden- thalassemia in two families were obtained from index tity with this abnormal hemoglobin was not estab- cases at Bellevue Hospital. The great majority of lished. This same component probably had been thalassemia trait cases were parents of children with observed severe Cooley's anemia. In all instances the diagnosis of by previous investigators employing the thalassemia was based on the hematological picture. classical Tiselius procedure in occasional speci- Several individuals who were suspected of having thalas- mens of blood from normal persons (2, 3) and semia were excluded from the study because of un- thalassemia patients (4), but had not been defined certain hematological findings. as a hemoglobin. The present report describes Zone electrophoresis was carried out by a slight modi- further properties of this hemoglobin fication of procedures described previously (5). A broad (designated starch slab, thinner than those usually used, was found A2 in this paper) with particular reference to its most suitable. The following dimensions were employed: constant presence in the blood of humans and 32 by 45 by 0.7 cm. The starch was washed over a filter certain primates and its elevation in individuals (with buffer only) prior to use. Barbital buffer pH 8.6 with thalassemia trait. r/2 0.05 was routinely employed. The hemoglobin solu- tion was applied to the slab by means of a capillary tube MATERIALS AND METHODS which was inserted in a slit 1 to 2 cm. in length in the starch which was kept just dry enough to prevent fu- Blood specimens were usually obtained in acid citrate sion of the slit. Numerous specimens could be applied dextrose or Alsever's solution. Hemolysates were pre- to a single slab in this manner (as many as 30 in three pared by the method of Drabkin without the use of rows in some experiments). Following application of AlC, (1). Following hemolysis the material was sub- one row of specimens, the slits were fused by means of jected twice to high speed centrifugation to insure re- buffer pipetted carefully on the starch several cm. on moval of all red cell ghosts. Special care was neces- either side of the row. A small spatula was used to sary in the preparation of the hemoglobin solutions be- flatten the site of application. The proper application of cause even a small number of ghosts in clear-appearing the hemoglobin in a thin band required considerable at- solutions interfered in the procedures of electrophoresis tention to details, but with some experience it was read- employed. The ghosts became adsorbed at the origin, ily possible. trapping hemoglobin, which thae gradually became re- For the demonstration and quantitation of the A, com- leased during the experiment causing a trail of hemo- ponent, the concentrated hemoglobin solutions obtained globin extending from the origin. Fresh blood samples by the Drabkin technique were used. For the quantitation were routinely converted to carboxyhemoglobin both and clear delineation of the abnormal hemoglobins, the before and again after the preparation of the hemolysates. concentrated solutions were diluted with two volumes of This was done by swirling the red cells or hemoglobin buffer. Three-tenths ml. of either the concentrated or solutions under a jet of CO in a large tube for approxi- dilute solution was usually applied. The starch slab was mately four minutes. The cyanmethemoglobin derivative covered with a polyethylene sheet which was applied with was used primarily for older specimens of blood or hemo- considerable care after blotting the block to remove ex- globin where partial conversion to methemoglobin had cess moisture. Too moist a block was avoided because occurred. To each 1-mL sample 0.05 ml. of freshly pre- of "melting" of the slab under the pressure of applica- pared 1 M potassium ferrcyanide and 0.05 mL of 1 M tion of the cover. The block was kept so that it would potassium cyanide were added. just adhere to the polyethylene under gentle pressure. Normal blood was obtained chiefly from laboratory The sheet was applied in such a manner as to force workers. Material from patients with various diseases out most of the air between it and the starch. The 1615 1616 H. G. KUNKEL, R. CEPPELLINI, U. MULLER-EBERHARD, AND J. WOLF separation was carried out for approximately 16 hours at This difference was found to be due primarily to con- 380 volts, giving a current without heating in the vicinity tamination of these preparations with non-colored proteins. of 85 ma. Following the separation, a dry towel was One experiment with a normal hemoglobin solution placed at both ends of the block after removal of the separated eight times as carboxyhemoglobin on the same cloth contacts to the electrode vessels. This blotting starch block is shown in Table I. The results for the procedure removed excess moisture that accumulated same material separated eight times on different starch during the separation and facilitated removal of the blocks are also illustrated. -In these experiments the re- polyethylene sheet and other manipulations of the starch sults are quite similar. However, there was no question block. The slab was then carefully viewed over a strong about the greater reproducibility using the same starch light which caused the red hemoglobin spots to stand out slab, and for accurate comparisons this procedure was very clearly. In work with the quantitation of the A2, usually employed. this spot was outlined with a thin spatula and the divi- Antisera for immunological analyses were produced sion from the main A component marked. The two seg- by injecting whole hemoglobin solutions from normal in- ments which included these components were partitioned dividuals. The Freund adjuvant technique was em- and removed from the lower polyethylene sheet, and each ployed in eight rabbits. Three of these showed weak was packed on a ground glass filter. Distilled water was antibodies against hemoglobin three months after injec- then added to displace the hemoglobin from the starch. tion. These were re-stimulated by the Freund technique A volume of water slightly greater than the volume of and potent antisera were obtained four weeks after the the packed starch was usually sufficient to remove all second injection. hemoglobin. With some preparations of starch a few Fetal hemoglobin was measured by the procedure of of the smaller particles passed through the filter. These Singer, Chernoff, and Singer (6, 7). Solubility studies were removed by centrifugation. The main A fraction were carried out by the procedure described by Green, was diluted to 20 times the volume of the A, fraction Cohn, and Blanchard (8). and each was measured in a Beckman spectrophotometer at 540 mA. The per cent concentration of the A, com- RESULTS ponent was obtained from these readings employing the dilution factor of 20. The protein was also determined I. Separation of hemoglobin A2 from solutions of on the same fractions by means of the modified Folin normal hemoglobin procedure (5). Hemoglobin A was used as the stand- ard for these measurements of color and protein concen- Figure 1 illustrates the protein curve obtained tration. The carboxyhemoglobin color procedure was after separation by zone electrophoresis of the routinely used but the cyanmethemoglobin method was very helpful in many instances. The two color procedures hemolysate from the red cells of a normal indi- gave very similar results. When the carbonmonoxy vidual. Two colored components are visible-the method was used, considerable care was necessary to main hemoglobin A and the small hemoglobin A2. keep the hemoglobin in the CO form. Partial forma- The latter is the subject of this report. In addi- tion of methemoglobin usually was greater for the A, tion, a third small peak is observed close to the component and gave low values. Direct protein analysis site of a gave values for the A2 component which were 5 to 10 application. This is colorless component per cent higher than by the hemoglobin color procedures. which showed some variation in concentration in different blood specimens and is the main non-he- TABLE I moglobin protein constituent of the red cells.' The Repeated analysis of same hemoglobin solution (normal) experiment illustrated in Figure 1 was carried out with carboxyhemoglobin and the color of the A, Hemoglobin As expressed as per cent of total hemoglobin component was clearly visible against the white Same Different starch starch starch background at the site of the A2 protein blocks blocks peak. Figure 2 shows the carboxyhemoglobin 2.41 2.51 color of the hemolysates from the blood of nine 2.51 2.33 normal individuals and two with sickle-cell trait.
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