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

Author:

MASRI M. S.1,JOSEPHSON AARON M.1,SINGER KARL1

Affiliation:

1. Department of Hematologic Research, Medical Research Institute, Michael Reese Hospital, Chicago, Ill.

Abstract

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.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Cited by 28 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Hemoglobin Ta-Li: β83 Gly→Cys;Biochimica et Biophysica Acta (BBA) - Protein Structure;1971-09

2. The A2 hemoglobin in hematological diseases;Clinica Chimica Acta;1970-06

3. Hemoglobin G Taiwan-Ami: α2β225 Gly → Arg;Biochemical and Biophysical Research Communications;1968-03

4. The identical structural anomalies of hemoglobins JMeinung and JKorat;Biochemical and Biophysical Research Communications;1966-09

5. Biosynthesis of Heme Proteins in Embryonic and Early Fetal Life;Proceedings of the Japan Academy;1966

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