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      • KCI등재후보

        한국산 감잎의 Polyphenol 화합물의 생리활성물질의 화학구조 및 효소저해효과

        안봉전,최희진,손준호,우희섭,한호석,박정혜,손규목,최청 한국식생활문화학회 2003 韓國食生活文化學會誌 Vol.18 No.5

        The lyophilization of the solution extracted from 60 percent of acetone applied to persimmon leaves, the compounding process in accordance with the solution's concentration, and the gel filteration through Sephadex G-50 of biologically activated substances obstructing enzyme activity, such as tyrosinase, xanthine oxidase, and angiotesin converting enzyme (ACE) led to the assumption that polyphenol was the compound serving as biologically activated substances obstructing enzyme activity. Xanthine oxidase involved in pruine metabolism oxidizes hypoxanthine to xanthine and xanthine to uric acid. In the continuous study for natural compound, nine flavan-3-ois have been isolated from the persimmon leaves. The structures of (+)-catechin, (+)-gallocatechin, procyanidin B-1, pyrocyanidin C-1, prodelphinidin B-3, gallocatechin-(4α→8)-catechin, procyanidin B-7-3-O-gallate, procyanidin C-1-3'-3''-3'''-O-trigallate and (-)-epigallocatechin-(4β→8)-epigallocatechin-(4β→8)-catechin were established by NMR and their inhibitory effect on xanthine oxidase activity was investigated. Procyanidin C-1-3'-3''-3'''-O-trigallate showed 94%, 90.69%, 80.90% inhibition at 100(μ)M and inhibited on the angiotension converting enzyme respectively. Procyanidin B-7-3-O-gallate and procyanidin 1-3'-3''-3'''-O-trigallate showed 66%, 63% inhibition at 100(μ)M and inhibited on the xanthine oxidase competitively. Procyanidin C-1-3'-3''-3'''-O-trigallate showed 70% inhibition at 100(μ)M inhibited on the thyrosinase competitively.

      • KCI등재후보

        들깨잎의 품종에 따른 성분분석 및 생리활성물질 탐색

        한호석,박정혜,최희진,손준호,김영활,김성,최청 한국식생활문화학회 2004 韓國食生活文化學會誌 Vol.19 No.1

        The biochemical components of Namcheondlggae, Miryangdlkkae 25, Boradlggae and Ipdlkkae 1 were measured. The samples were extracted with hot water, 60% acetone or 80% ethanol for screening physiological activity. The crude protein content (4.36%) was found in the Miryangdlkkae 25 and calcium content (497.5 mg%) was found in the Namcheondlggae among the tested 4 perilla leaves. Fructose was 30.86 mg% in the Namcheondlggae and free amino acids at all perilla leaves was detected seventeen. In Boradlggae, glutamic acid and alanin were 25.37 and 11.91 mg%. Totally nine non-volatile organic acids were also detected and the contents of malic acid and glutaric acid were 28.34 and 14.57 mg% in Boradlggae. The Miryangdlkkae 25 had the highest vitamin C amount which was 113.24 mg%. Angiotensin converting enzyme (ACE) inhibition activity of 80% ethanol extract of Boradlggae was 46.71%. Electron donating activity of 60% acetone extract from Namcheondlggae was the strongest inhibition activity as 98.19% when 200ppm level of the sample extracts were added.

      • SCOPUSKCI등재

        Serratia liquefaciens AL-11이 생산하는 Alkaline Lipase의 특성 및 작용양상

        최청,김태완,안봉전,김영활,손준호,김성,최희준 한국미생물생명공학회 ( 구 한국산업미생물학회 ) 1996 한국미생물·생명공학회지 Vol.24 No.1

        본 효소의 최적 반응온도는 약 45℃이고, 최적 pH는 10.0 정도였고, pH 7.0~10.0 범위와 30~50℃의 범위에서 안정하였다. 금속이온중 Mn^2+, Ca^2+ 등에 의하여 활성이 증대되었으나 Fe^2+, Pb^2+와 Zn^2+ 등에 의해서는 효소 활성이 저해되었고, 효소활성 저해제 중 ethylenediaminetetraacetic acid(EDTA)에 의해 강한 저해작용을 나타내어 본 효소는 효소분자 중 금속이온이 관여하는 것으로 추정되었다. 효소반응 처리한 olive oil 가수분해물을 박충크로마토그래피 분석한 결과 Serratia liquefaciens AL-11이 생산하는 지방분해효소는 기질특이성이 비특이적이었으며, sodium cholate, sodium edoxychol-ate, sodium taurocholate 등의 담즙산염에 의해 효소활성이 증대되었다. The optimum temperature and pH for the enzyme activity were 45℃ and 10.0, respectively. The enzyme was stable in a pH range of 5 to 10, and 62% of its activity was lost on heat treatment at 60℃ for 20 min. The activity of the purified enzyme was inhibited by Fe^2+, Zm^2+ and Pb^2+, and slightly activated by Mn^2+ and Ca^2+. γ-Chloromercuribenzoic acid, 2,4-dinitrophenol and H_2O_2 did not show inhibitory effect on the lipolytic activity of the alkaline lipase but ethylenediaminetetraacetic acid inhibited the enzyme activity. This suggested that the enzyme have metal group in its active site. Sodium salts of bile acids stimulated the enzyme activity. Analysis of hydrolyzates of olive oil after the lipase reaction revealed that Serratia liquefaciens AL-11 produced non-specific lipolytic enzyme.

      • 과일과피로부터 폴리페놀 분리에 따른 생리기능연구

        안봉전,이진태,곽재훈,박정미,이진영,박태순,손준호,최청 경산대학교 생명자원개발연구소 2003 생명자원과 산업 Vol.7 No.-

        Biological activities and anticarcinogenicity of Korean Pear peel were investigated. Electron donating activity and superoxide dismutase(SOD)-like activity of fraction Ⅱ, Ⅲ were up to 90% and 50-60% at 50ppm, respectively. Inhibitory effects on xanthine oxidase were about 80% at 50ppm, breast adenocarcinoma was about 60% at 2,000 ppm, higher Ⅲ than Ⅱ. Inhibitory effect on prostate adenocarcinoma was about 23% at 500 ppm. In conclusion, Korean Pear peel was expected to use as a functional material.

      • 한국산 약용식물의 화장품천연소재로서 응용에 관한연구

        안봉전,이진태,이순애,곽재훈,박정미,이진영,박태순,손준호 경산대학교 생명자원개발연구소 2003 생명자원과 산업 Vol.7 No.-

        Biological activities and application of sanguisorbae officinalis L. were investigated. In the enzymological physiological activities, the electron donating ability(EDA) was 54.92% in 10 ppm and it was over 90% over 50ppm and SOD-like activity was high as 65.36% in 1000 ppm, it was gradual increased. As inhibitory effect of xanthine oxidase, it was 17.90% in 200 ppm and a little low as 36.89% in 500 ppm and inhibitory effect of tyrosinase, it was a little low as 20.45% below 1000 ppm. As the result of measuring the lipid oxidation, all the concentrations of medical ion treatments had the ability to keep it from acidification and metal ion blocking effects about the lipid oxidation promoting factors(Fe^(2+) and Cu^(2+)), Fe^(2+) was better than Cu^(2+) and all concentrations of medical ion treatments was 40% in 50ppm. When it was applied into normal skin-softener it showed safe effect so that we can expect that as the natural material of cosmetics.

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