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Amino Acid Sequence in All the Tryptic Peptides from the α Polypeptide Chain of All Component ot Chicken Hemoglobin

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Title: Amino Acid Sequence in All the Tryptic Peptides from the α Polypeptide Chain of All Component ot Chicken Hemoglobin
Authors: Wu, Kuchayu
Authors (alternative): 呉, 谷喬
Issue Date: 25-Oct-1969
Citation: Acta medica Nagasakiensia. 1969, 14(1-2), p.42-71
Abstract: Hemoglobin was obtained from blood of adult white leghorns. It was first separated into three components, AI, AII, and AIII by CMC-column chromatography. AII, the greatest component of the three was chosen as the subject matter of the present study. It was first converted into globin by removal of heme in acetone-HCl solution, and then the globin was separated into α andβ polypeptide chains by Amberlite CG50 column chromatography. The α polypeptide chain was digested with trypsin, and tryptic peptides thus obtained were subjected to column chromatography and then to paper chromatography for isolation and purification. The column chromatography was carried out by using Dowex 1X2 as the adsorbent and the acetate buffer containing organic bases such as pyridine, collidine, lutidine, and picoline as the developer. The developer for the paper chromatography was the mixture of n-butanol, acetic acid, and water. The amino acid composition of the tryptic peptides thus isolated and purified was analyzed on an amino acid analyzer and subsequently the amino acid sequence in these tryptic peptides was determined by using partial hydrolyses with various enzymes, the PTC method, and the DNP method. The results were discussed in comparison with human hemoglobin. As a result, replacement of amino acids in the tryptic peptides between adult human and white leghorn hemoglobins was presumed at 35 positions in the α polypeptide chain.
URI: http://hdl.handle.net/10069/15555
ISSN: 00016055
Type: Departmental Bulletin Paper
Text Version: publisher
Appears in Collections:Volume 14, No. 1-2

Citable URI : http://hdl.handle.net/10069/15555

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