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      SCIE SCOPUS KCI등재

      동물 경조직 단백 성분의 조성과 생리기능에 관한 연구 우각 수우각 서각에서 분리한 경단백의 조성에 대하여 = Studies on the Compostions of Hard Tissue Proteins Extracted from Bovine Horn , Water Buffalo Horn and Rhinoceros Horn

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      https://www.riss.kr/link?id=A3289953

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      We have previously reported that the abstinence syndrom of narcotic addicts was relieved by the protein extracts of animal hard tissue (from Manis pentadactyla). The protein extracts of the hard tissue were found to be a sort of keratin. Keratins were extracted from three species of animal horns (bovine horn, water buffalo horn and rhinoceros horn) with 0.1 M-Thioglycolate at 40℃ and S-carboxymethyl derivatives (SCMK) of the keratin were synthesized by the method of Gillespie and his co-workers. The yields of the keratin derivatives were in the range of 16% to 30% of the dryweight of the horns. In an attempt to elucidate and compare the compositions of the keratin derivatives, the analysis for amino acids, monosaccharides, hexosamines, uronic acids, sialic acids among bovine horn, water buffalo horn, and rhinoceros horn, were performed. Eighteen kinds of amino acids were found in the three keratin derivatives and there were no differences in the composition among them, with the exception of lysine contents of bovine horn protein extracts(2.67%), which was distinctively lower than those of water buffalo horn protein extracts(5.57%) and those of rhinoceros horn protein extracts (4.99%). The amounts of carboxymethyl cysteine of bovine horn are twice of those of water buffalo horn and those of rhinoceros horn. In view of these results, it is presumed that the crosslinking rate of bovine horn keratin by cystine disulfide bridge is higher than those of water buffalo horn and Rhinoceros horn. The conjugated components of the keratin derivatives, such as monosaccharides, sialic acids, hexosamines, and uronic acids were totally contained 1.38% in bovine horn keratin, 0.47% in water buffalo horn keratin and 1.04 in rhinoceros horn keratin. There are some similarities among the keratin derivatives of the three species, such as these keratins do not contain galactosamine but glucosamine, and also the existance of glucuronic acid in these keratins is not detected but galacturonic acid. The sugar moieties of these proteins consisted of glucose, galactose, xylose, fucose in bovine horn protein extracts; glucose, galactose, xylose, fucose in water buffalo horn protein extracts; glucose, galactose, mannose, ribose in rhinoceros horn protein extracts.
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      We have previously reported that the abstinence syndrom of narcotic addicts was relieved by the protein extracts of animal hard tissue (from Manis pentadactyla). The protein extracts of the hard tissue were found to be a sort of keratin. Keratins wer...

      We have previously reported that the abstinence syndrom of narcotic addicts was relieved by the protein extracts of animal hard tissue (from Manis pentadactyla). The protein extracts of the hard tissue were found to be a sort of keratin. Keratins were extracted from three species of animal horns (bovine horn, water buffalo horn and rhinoceros horn) with 0.1 M-Thioglycolate at 40℃ and S-carboxymethyl derivatives (SCMK) of the keratin were synthesized by the method of Gillespie and his co-workers. The yields of the keratin derivatives were in the range of 16% to 30% of the dryweight of the horns. In an attempt to elucidate and compare the compositions of the keratin derivatives, the analysis for amino acids, monosaccharides, hexosamines, uronic acids, sialic acids among bovine horn, water buffalo horn, and rhinoceros horn, were performed. Eighteen kinds of amino acids were found in the three keratin derivatives and there were no differences in the composition among them, with the exception of lysine contents of bovine horn protein extracts(2.67%), which was distinctively lower than those of water buffalo horn protein extracts(5.57%) and those of rhinoceros horn protein extracts (4.99%). The amounts of carboxymethyl cysteine of bovine horn are twice of those of water buffalo horn and those of rhinoceros horn. In view of these results, it is presumed that the crosslinking rate of bovine horn keratin by cystine disulfide bridge is higher than those of water buffalo horn and Rhinoceros horn. The conjugated components of the keratin derivatives, such as monosaccharides, sialic acids, hexosamines, and uronic acids were totally contained 1.38% in bovine horn keratin, 0.47% in water buffalo horn keratin and 1.04 in rhinoceros horn keratin. There are some similarities among the keratin derivatives of the three species, such as these keratins do not contain galactosamine but glucosamine, and also the existance of glucuronic acid in these keratins is not detected but galacturonic acid. The sugar moieties of these proteins consisted of glucose, galactose, xylose, fucose in bovine horn protein extracts; glucose, galactose, xylose, fucose in water buffalo horn protein extracts; glucose, galactose, mannose, ribose in rhinoceros horn protein extracts.

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