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• W2022083092 abstract "five components in the adult, four of which contain N-acetyl amino acids. The results of the present investigation show that the adult chicken contains a minimum of five components, and these differ from one another primarily in the structure of one polypeptide subunit. The five-day embryo possesses at least three distinct Hb types, and these embryonic Hb types differ from the adult in the structure of both polypeptide subunit classes. A large number of distinct genetic loci may specify the primary structure of Hb subunits at one time or another during the life of the chicken. Materials and Methods.-Adults and eggs of white Leghorn chickens were obtained from Kimber Farms, Niles, California. Erythrocytes were collected and hemolyzed by conventional techniques.2 Separation of adult Hb's was carried out by carboxymethylcellulose (CMC, Brown and Co., 0.8 mEq/gm) chromatography essentially as outlined by Matsuda and Takei.5 One of the adult Hb components (named A-2) thus separated was found later to consist of two components, which were separated by executing a vertical starch gel electrophoresis as specified by Manwell,6 as a preparative technique. Embryonic Hb's, on the other hand, were satisfactorily separated only by the gel electrophoresis. Extraction of separated components from the gel was done by freezing and thawing macerated portions of the gels in dilute borate buffer. The gel electrophoresis was used also for examination of purity of isolated Hb components. Hb concentration was determined by absorption of the cyanomethemoglobin derivative (CNmetHb) at 540 m, (molar extinction = 11.5 X 103).7 Hb solutions were concentrated by ammonium sulfate precipitation or dialysis against 10-20 per cent polyethylene glycol in 0.03 M borate, pH 8.6, containing 0.01 per cent cyanide. Globin was prepared by the acid-acetone method.8 Chromatographic separation of Hb subunits at pH 1.9 was carried out as described by Muller.9 Separation of Hb subunits at pH 1.9 by starch gel electrophoresis was accomplished by the method of MIuller.9 Starch gels were stained for protein using amido black and for Hb using o-diansidine. Polyacrylamide gel electrophoresis at pH 8.9 was carried out according to directions of the manufacturer (Canalco Corp.)." @default.
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• W2022083092 title "The heterogeneity of chicken hemoglobin." @default.
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• W2022083092 doi "https://doi.org/10.1073/pnas.56.5.1477" @default.
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