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Isolation of All Soluble Tryptic Peptides from the α Polypeptide Chain of Adult Hemoglobin from Japanese Monkey (Macaca fuscata fuscata) and their Amino Acid Compositions


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Title: Isolation of All Soluble Tryptic Peptides from the α Polypeptide Chain of Adult Hemoglobin from Japanese Monkey (Macaca fuscata fuscata) and their Amino Acid Compositions
Authors: Terao, Yoji
Authors (alternative): 寺尾, 洋治
Issue Date: 25-Mar-1969
Citation: Acta medica Nagasakiensia. 1969, 13(3-4), p.170-182
Abstract: The adult Japanese monkey (macaca fuscata fuscara) hemoglobin was converted into globin by removal of heme. The globin was separated into α and,β polypeptide chains by countercurrent distribution with the solvent system of trichloroacetic acid containing sec-butanol, propionic acid, and water. The α polypeptide chain was hydrolyzed with trypsin. From the hydrolysate, peptides soluble at the adjustment of pH to 6.4 were isolated by column chromatography on Dowex 1 * 2 with acetate buffer containing organic bases such as pyridine, collidine, lutidine, and picoline, and then purified by descending paper chromatography with the mixture of n-butanol, acetic acid, and water. The amino acid compositions of the peptides thus isolated and purified were analyzed after HCl hydrolysis. The results were discussed in comparison with adult human hemoglobin and rhesus monkey (macaca mulatta) hemoglobin. Concerning the amino acid compositions of the soluble tryptic peptides from the α polypeptide chain, it is presumed, that Japanese monkey hemoglobin is different from human hemoglobin in four amino acids of the three peptides, but quite the same with rhesus monkey hemoglobin which belongs to the same genus as the Japanese monkey does.
URI: http://hdl.handle.net/10069/15546
ISSN: 00016055
Type: Departmental Bulletin Paper
Text Version: publisher
Appears in Collections:Volume 13, No. 3-4

Citable URI : http://hdl.handle.net/10069/15546

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