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Volumn 172, Issue , 2015, Pages 261-264

Comparative analysis of procoagulant and fibrinogenolytic activity of crude protease fractions of turmeric species

Author keywords

Curcuma longa Linn; Fibrinogenolytic; Hemostasis; Pro coagulant; Serine protease(s)

Indexed keywords

PROCOAGULANT; PROTEINASE; TURMERIC; COAGULATING AGENT; FIBRINOGEN; PEPTIDE HYDROLASE; PLANT EXTRACT; SERINE PROTEINASE;

EID: 84936998717     PISSN: 03788741     EISSN: 18727573     Source Type: Journal    
DOI: 10.1016/j.jep.2015.06.018     Document Type: Article
Times cited : (18)

References (16)
  • 1
    • 0018257842 scopus 로고
    • Antimicrobial efficacy of essential oil of Curcuma longa
    • A. Banerjee, and S.S. Nigam Antimicrobial efficacy of essential oil of Curcuma longa Indian J. Med. Res. 68 1978 864 866
    • (1978) Indian J. Med. Res. , vol.68 , pp. 864-866
    • Banerjee, A.1    Nigam, S.S.2
  • 2
    • 33745833243 scopus 로고    scopus 로고
    • Plant medicines of Indian origin for wound healing activity: A review
    • T.K. Biswas, and B. Mukherjee Plant medicines of Indian origin for wound healing activity: a review Int. J. Low. Extrem. Wounds 2 2003 25 39
    • (2003) Int. J. Low. Extrem. Wounds , vol.2 , pp. 25-39
    • Biswas, T.K.1    Mukherjee, B.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram of protein utilizing the principle dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram of protein utilizing the principle dye binding Anal. Biochem. 7 1976 248 254
    • (1976) Anal. Biochem. , vol.7 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0020587190 scopus 로고
    • Anticoagulant activity and plasma phosphatidylserine hydrolysis by snake venom phospholipases A2
    • E. Condrea, C.C. Yang, and P. Rosenberg Anticoagulant activity and plasma phosphatidylserine hydrolysis by snake venom phospholipases A2 Thromb. Haemost. 49 1983 151 157
    • (1983) Thromb. Haemost. , vol.49 , pp. 151-157
    • Condrea, E.1    Yang, C.C.2    Rosenberg, P.3
  • 7
    • 0036190104 scopus 로고    scopus 로고
    • The chemopreventive compound curcumin is an efficient inhibitor of Epstein-Barr virus BZLF1 transcription in Raji DR-LUC cells
    • M. Hergenhahn, U. Soto, A. Weninger, A. Polack, C.H. Hsu, A.L. Cheng, and F. Rosl The chemopreventive compound curcumin is an efficient inhibitor of Epstein-Barr virus BZLF1 transcription in Raji DR-LUC cells Mol. Carcinog. 33 2002 137 145
    • (2002) Mol. Carcinog. , vol.33 , pp. 137-145
    • Hergenhahn, M.1    Soto, U.2    Weninger, A.3    Polack, A.4    Hsu, C.H.5    Cheng, A.L.6    Rosl, F.7
  • 8
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • C. Heussen, and E.B. Dowdle Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates Anal. Biochem. 102 1980 196 202
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0000762571 scopus 로고
    • Studies on snake venom: XII. Distribution of proteinase activities among Japanese and Formosan snake venoms
    • Y. Murata, M. Satake, and T. Suzuki Studies on snake venom: XII. Distribution of proteinase activities among Japanese and Formosan snake venoms J. Biochem. 53 1963 431 437
    • (1963) J. Biochem. , vol.53 , pp. 431-437
    • Murata, Y.1    Satake, M.2    Suzuki, T.3
  • 11
    • 70450057690 scopus 로고    scopus 로고
    • Purification and properties of cysteine protease from rhizomes of Curcuma longa (Linn.)
    • R. Nagarathnam, A. Rengasamy, and R. Balasubramanian Purification and properties of cysteine protease from rhizomes of Curcuma longa (Linn.) J. Sci. Food Agric. 90 2010 97 105
    • (2010) J. Sci. Food Agric. , vol.90 , pp. 97-105
    • Nagarathnam, R.1    Rengasamy, A.2    Balasubramanian, R.3
  • 12
    • 0017231072 scopus 로고
    • Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom
    • C. Ouyang, and C.M. Teng Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom Biochim. Biophys. Acta 420 1976 298 308
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 298-308
    • Ouyang, C.1    Teng, C.M.2
  • 13
    • 84937002840 scopus 로고    scopus 로고
    • Hemostatic, milk clotting and blood stain removal potential of cysteine proteases from Calotropis gigantea (L.) R. Br. Latex
    • S.B. Omana, and K.S Maheshwari Hemostatic, milk clotting and blood stain removal potential of cysteine proteases from Calotropis gigantea (L.) R. Br. Latex Pharmacogn. Mag. 10 2014 350 356
    • (2014) Pharmacogn. Mag. , vol.10 , pp. 350-356
    • Omana, S.B.1    Maheshwari, K.S.2
  • 16
    • 84937000598 scopus 로고    scopus 로고
    • Turmeric: The Indian culinary delight to the world
    • L. Srinivas, and M. Chethankumar Turmeric: the Indian culinary delight to the world Indian J. Nutr. Diet. 43 2006 169 173
    • (2006) Indian J. Nutr. Diet. , vol.43 , pp. 169-173
    • Srinivas, L.1    Chethankumar, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.