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Isolation and properties of γ chain from human fetal hemoglobin
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Description
Abstract 1. 1. Dissociation of human fetal hemoglobin (FII fraction) into its constituent subunits was investigated electrophoretically. 2. 2. A simple method of isolating the γ chain from fetal hemoglobin is described. The procedure is a slight modification of the method of Bucci and Fronticelli 1 for adult hemoglobin, consisting of p-chloromercuribenzoate treatment at pH 4.7 and fractionation by CM-cellulose column chromatography. 3. 3. One of the three fractions obtained by this method was identified as the γ chain by means of electrophoretic behavior, ultraviolet absorption spectra, alkali resistance and amino-terminal amino acid analysis. The yield of γ chain was 40–60%.
Journal
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- Biochimica et Biophysica Acta (BBA) - Protein Structure
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Biochimica et Biophysica Acta (BBA) - Protein Structure 175 41-48, 1969-02-01
Elsevier BV
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Details 詳細情報について
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- CRID
- 1870302167945595904
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- ISSN
- 00052795
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- Data Source
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- OpenAIRE