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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 441 - 450 (10page)
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초록· 키워드
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Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from the skin of hybrid Clarias sp. with the yields of $18.11{\pm}0.32$ and $26.69{\pm}0.54%$ (wet weight basis), respectively. Both collagens were characterized as type I collagen, containing ${\alpha}1$ and ${\alpha}2$ chains. Presence of high molecular weight crosslinks were observed in the gel electrophoresis of both collagens. Fourier transform infrared spectra of both collagens were almost similar, suggesting that pepsin hydrolysis did not disrupt the triple helical structure. The amino acid analysis showed glycine was the most abundant, with 207/1000 and 223/1000 residues present in ASC and PSC, respectively. The amounts of imino acids were 185/1000 residues for both. Thermal denaturation temperatures were determined to be 31.5 and $31.0^{\circ}C$, respectively. Both collagens exhibited high solubility in acidic pH (1-5) and below 4% (w/v) NaCl concentration.
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