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Some Notes On The Starch-Gel Electrophoresis Of Hemoglobins



Some Notes On The Starch-Gel Electrophoresis Of Hemoglobins



Journal of Laboratory and Clinical Medicine 63: 290-296



Starch-gel electrophoresis of hemoglobin solutions was carried out in 2 different buffer systems of approximately the same pH. The tris-citrate buffer was noted to provide sharp definition of the more slowly moving hemoglobins at pH 8.7 but was inadequate for the separation of Hgb F from Hgb A. Methemoglobin forms of various hemoglobin types moved more slowly than the oxy, reduced, CO, or cyanmethemoglobin compounds. Electrophoresis in a lithium buffer system, pH 8.04, provided sharp definitions of hemoglobins with a mobility equal to or greater than that of Hgb S, permitted a sharp distinction of Hgb F from Hgb A and demonstrated an even more striking displacement cathodally of the methemoglobin forms of the various hemoglobin types.

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Accession: 025489346

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PMID: 14125115


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