韓國人에서 發見된 異常血色素의 構造 分析에 關한 硏究 = Study on the Structural Analysis of Abnormal Hemoglobin in Korean

다국어 초록 (Multilingual Abstract)

To study the structural analysis of abnormal α-chain of hemoglobin in Koreaan, at first, it was identifed by agar gel electrophresis, isoelectric focusing and Supersepraphore Ⅲ polyacetate membrane electrophoresis. In order to purift the abnormal α-chain in significant amounts, CM-cellulose chromatography would be used. The purified abnormal α-chain was then carboxymethylated and submitted to tryptic digestion. The peptide mixture was separated by Sephadex G－25 gel filtration chromatography. And then the peptide fractions, designated TG1, TG2, TG3 and TG4, were analyzed by finger printing on silica gel plate. TG4 among the peptide fraction contained a unique peptide, designated peptide A. After the extraction of peptide A from the silica gel plate, the amino acid analysis was performed.
The results were obtained as follows.
1. The separation of normal, abnormal and cord hemoglobing were performed and differentiated easily by Supersepraphore Ⅲ polyacetate membrane electrophoresis, urea-TEB buffer, pH 6.3
2. The content of abnormal α-chain in total α-chain was amount to 22%, and considered to be heterozygous mutant with abnormality in one of the four α-genes.
3. The tryptic peptides of TG4 from abnormal α-chain could be separated by finger printing on silica gel plate, and revealed the presence of an unique peptide A which was not appeared in normal α-chain.
4. This peptide, TG4, was determined the amino acide contents by amino acid analyzer, The peptide A contained 5 amino acids, asn(14.04 mol%), arg(20.94 mol%), thr(24.42 mol%), pro(20.11 mol%) and 1ys(20.08 mol%).