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

국문 초록 (Abstract)

동물 경조직 단백에 관한 연구의 일환으로 3종의 동물의 각질(우각, 수우각, 서각)을 각각 채취하여 Gillespie 등의 방법에 의하여 0.1 M-thioglycolate로 $400^{\circ}C$에서 keratin을 추출한 후 S-carboxymethyl (SCMK) 유도체를 합성하였고 $\frac{1}{10}$ N-HCl 로 등전점 (pI 4.7~5.05)의 범위에서 침전된 단백을 각각 분리하였다. 추출된 경단백의 수득량은 건조 중량으로 16~30%이었다. 추출된 keratin의 아미노산 조성은 3종 공히 18종이었으며, 그 조성비의 차이는 별로 없었으나 단 우각에서 추출된 단백질의 Lysine 함량은 2.67%로 수우각 5.57%, 서각 4.99%에 비하여 현저한 차이가 있었으며, 우각의 S-carboxymethyl cysteine의 함량은 9.41%로 수우각 6.06%, 서각 5.96%에 비해 크므로 우각 keratin의 disulfide bridge에 의한 cross-linking 정도가 수우각, 서각에 비해 크다는 것 을 나타내고 있다. 추출 단백의 monosaccharide, sialic acid, hexosamine, 및 uronic acid의 조성을 분석한 결과 이들 총 함량을 표시하면 추출 단백질의 건조중량에 대하여 우각은 1.38%, 수우각 0.47%, 서각 1.04%이었다. Sialic acid의 함량은 추출 단백의 건조중량에 대하여 gm 당 우각 $1.26{\mu}mol$, 수우각 $0.29{\mu}mol$, 서각 $0.96{\mu}mol$로 나타났다. Hexosamine 분석에서 3종 공히 galactosamine은 검출 되지 않고 glucosamine만이 검출?瑛만? 또한 uronic acid 분석결과 glucuronic acid는 3종 공히 검출되지 않았고 galacturonic acid만이 검출되었다. 또한 중성당의 조성은 우각 및 수우각에는 glucose, galactose, xylose, fucose가 서각에는 glucose, mannose, ribose가 각각 검출되었다.

다국어 초록 (Multilingual Abstract)

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 $40^{\circ}C$ 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 dry weight 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, mannose, ribose in rhinoceros horn protein extracts.