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    Distribution of chitinases and characterization of two chitinolytic enzymes from one-year-old Korean Ginseng (Panax ginseng C.A. Meyer) roots = Distribution of chitinases and characterization of two chitinolytic enzymes from one-year-old Korean Ginseng (Panax ginseng C.A. Meyer) roots

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    https://www.riss.kr/link?id=A82503514

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    다국어 초록 (Multilingual Abstract) kakao i 다국어 번역

    We report the tissue-specific distribution of chitinolytic activity in Korean ginseng root and characterize two 31-kDa chitinolytic enzymes. These two enzymes (SBF1 and SBF2) were purified 70- and 81-fold with yields of 0.75 and 1.25%, respectively, and exhibited optimal pH and temperature ranges of 5.0-5.5 and 40-50℃. With [3H]-chitin as a substrate, Km and Vmax values of SBF1 were 4.6 mM and 220 mmol/mg-protein/h, respectively, while those of SBF2 were 7.14 mM and 287 mmol/mg-protein/h. The purified enzymes showed markedly less activity with p-nitrophenyl-N-acetylglucosaminide and fluorescent 4-methylumbelliferyl glycosides of D-N-acetylglucosamine oligomers than with [3H]-chitin. End-product inhibition of both enzymes demonstrated that both are endochitinases with different N-acetylglucosaminidase activity. Furthermore, the NH2-terminal sequence of SBF1 showed a high degree of homology with other plant chitinases whereas the NH2-terminal amino acid of SBF2 was blocked. [BMB reports 2010; 43(11): 726-731]
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    We report the tissue-specific distribution of chitinolytic activity in Korean ginseng root and characterize two 31-kDa chitinolytic enzymes. These two enzymes (SBF1 and SBF2) were purified 70- and 81-fold with yields of 0.75 and 1.25%, respectively, a...

    We report the tissue-specific distribution of chitinolytic activity in Korean ginseng root and characterize two 31-kDa chitinolytic enzymes. These two enzymes (SBF1 and SBF2) were purified 70- and 81-fold with yields of 0.75 and 1.25%, respectively, and exhibited optimal pH and temperature ranges of 5.0-5.5 and 40-50℃. With [3H]-chitin as a substrate, Km and Vmax values of SBF1 were 4.6 mM and 220 mmol/mg-protein/h, respectively, while those of SBF2 were 7.14 mM and 287 mmol/mg-protein/h. The purified enzymes showed markedly less activity with p-nitrophenyl-N-acetylglucosaminide and fluorescent 4-methylumbelliferyl glycosides of D-N-acetylglucosamine oligomers than with [3H]-chitin. End-product inhibition of both enzymes demonstrated that both are endochitinases with different N-acetylglucosaminidase activity. Furthermore, the NH2-terminal sequence of SBF1 showed a high degree of homology with other plant chitinases whereas the NH2-terminal amino acid of SBF2 was blocked. [BMB reports 2010; 43(11): 726-731]

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    참고문헌 (Reference)

    1 Yamamot, M., "Stimulatory effect of Panax ginseng principles on DNA and protein synthesis in rat testes" 27 : 1404-1405, 1977

    2 Han, B. K., "Purification and characterization of acidic chitinases from gizzards of broiler (Gallus gallus L.)" 33 : 326-331, 2000

    3 Yu, Y. H., "Problems and present states of researches on ginseng diseases in Korea" 120-130, 1994

    4 Emanuelsson, O., "Locating proteins in the cell using TargetP, SignalP and related tools" 2 : 953-971, 2007

    5 Lam, S. K., "Isolation of a small chitinase-like antifungal protein from Panax notoginseng (Sanchi ginseng) roots" 33 : 287-292, 2001

    6 Konno, C., "Isolation and hypoglycemic activity of panazans A, B, C, D and E glycans of Panax ginseng roots" 50 : 434-436, 1984

    7 Chen, Z. K., "Isolation and characterization of a group of oligopeptides related to oxidized glutathione from the root of Panax ginseng" 52 : 137-142, 1998

    8 Pulla, R. K., "Identification and characterization of class I chitinase in Panax ginseng C. A. Meyer" Mol. Biol. Rep. (in press) 2010

    9 Lee, Y. J., "Ginsenoside-Rg1, one of the major active molecules from Panax ginseng, is a functional ligand of glucocorticoid receptor" 133 : 135-140, 1997

    10 Kang, S. Y., "Ginsenoside-Rg1 regulates the induction of tyrosine aminotransferase gene transcription in rat hepatocyte cultures" 205 : 1696-1701, 1994

    1 Yamamot, M., "Stimulatory effect of Panax ginseng principles on DNA and protein synthesis in rat testes" 27 : 1404-1405, 1977

    2 Han, B. K., "Purification and characterization of acidic chitinases from gizzards of broiler (Gallus gallus L.)" 33 : 326-331, 2000

    3 Yu, Y. H., "Problems and present states of researches on ginseng diseases in Korea" 120-130, 1994

    4 Emanuelsson, O., "Locating proteins in the cell using TargetP, SignalP and related tools" 2 : 953-971, 2007

    5 Lam, S. K., "Isolation of a small chitinase-like antifungal protein from Panax notoginseng (Sanchi ginseng) roots" 33 : 287-292, 2001

    6 Konno, C., "Isolation and hypoglycemic activity of panazans A, B, C, D and E glycans of Panax ginseng roots" 50 : 434-436, 1984

    7 Chen, Z. K., "Isolation and characterization of a group of oligopeptides related to oxidized glutathione from the root of Panax ginseng" 52 : 137-142, 1998

    8 Pulla, R. K., "Identification and characterization of class I chitinase in Panax ginseng C. A. Meyer" Mol. Biol. Rep. (in press) 2010

    9 Lee, Y. J., "Ginsenoside-Rg1, one of the major active molecules from Panax ginseng, is a functional ligand of glucocorticoid receptor" 133 : 135-140, 1997

    10 Kang, S. Y., "Ginsenoside-Rg1 regulates the induction of tyrosine aminotransferase gene transcription in rat hepatocyte cultures" 205 : 1696-1701, 1994

    11 Toda, N., "Ginsenoside potentiates NO-mediated neurogenic vasodilatation of monkey cerebral arteries" 76 : 109-113, 2001

    12 Kim, S. I., "Extraction and purification of ginseng oligopeptides with antilipolytic activities" 30 : 88-94, 1987

    13 Kajiwara, H., "Evidence of metal binding activities of pentadecapeptide from Panax ginseng" 687 : 443-448, 1996

    14 Park, H. J, "Effect of non-saponin fraction from Panax ginseng on cGMP and thromboxane A2 in human platelet aggregation" 49 : 157-162, 1995

    15 Yagi, A., "Effect of a peptide from Panax ginseng on the proliferation of baby hamster kidney-21 cells" 60 : 171-173, 1994

    16 Baek, J. H., "Distribution of chitinases in rice (Oryza sativa L) seed and characterization of a hull-specific chitinase" 34 : 310-315, 2001

    17 Trudel, J., "Detection of chitinase activity after polyacrylamide gel electrophoresis" 178 : 362-366, 1989

    18 Laemmli, U. K., "Cleavage of structural proteins during the assembly of the head protein of bacteriophage T4" 227 : 680-685, 1970

    19 Ohtakara, A., "Chitinase and β-N-acetylhexosaminidase from Pycnoporus cinnabarinus" 161 : 462-470, 1989

    20 Tomoda, M., "Characterization of two acidic polysaccharides having immunological activities from the root of Panax ginseng" 16 : 22-25, 1993

    21 McCreath, K. J., "A rapid and sensitive microassay for determination chitinolytic activity" 14 : 229-237, 1992

    22 Molano, J., "A rapid and sensitive assay for chitinase using tritiated chitin" 83 : 648-656, 1977

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    연월일 이력구분 이력상세 등재구분
    학술지등록 한글명 : BMB reports
    외국어명 : BMB reports
    2024 평가 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
    2021-01-01 등재 등재학술지 선정 (해외등재 학술지 평가) KCI등재
    2020-12-01 등재 등재후보로 하락 (해외등재 학술지 평가) KCI등재후보
    2013-07-17 학술지명변경 한글명 : BMB reports -> BMB Reports
    외국어명 : BMB reports -> BMB Reports
    KCI등재
    2011-01-01 등재 등재학술지 유지 (등재유지) KCI등재
    2009-09-21 학회명변경 한글명 : 대한생화학ㆍ분자생물학회 -> 생화학분자생물학회
    영문명 : Korean Society Of Medical Biochemistry And Molecular Biology -> Korean Society Of Biochemistry And Molecular Biology
    KCI등재
    2009-01-01 등재 등재학술지 유지 (등재유지) KCI등재
    2007-01-01 등재 등재학술지 유지 (등재유지) KCI등재
    2005-01-01 등재 등재학술지 유지 (등재유지) KCI등재
    2002-01-01 등재 등재학술지 선정 (등재후보2차) KCI등재
    1999-07-01 등재 등재후보학술지 선정 (신규평가) KCI등재후보
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    기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
    2016 2.76 0.5 1.94
    KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
    1.45 1.12 0.646 0.12
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