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Volumn 133, Issue 3, 2012, Pages 835-841

Anticoagulant activities of goby muscle protein hydrolysates

Author keywords

Activated partial thromboplastin time; Anticoagulant peptides; Goby; Protein hydrolysates; Thrombin time

Indexed keywords

ACTIVATED PARTIAL THROMBOPLASTIN TIME; ALKALINE PROTEASE; AMINO ACID SEQUENCE; ANTICOAGULANT ACTIVITIES; BACILLUS LICHENIFORMIS; CRUDE PROTEASE; ESI-MS/MS; GOBY; MUSCLE PROTEINS; PROTEIN HYDROLYSATE; PROTEIN HYDROLYSATES; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SEPHADEX; THROMBIN TIME;

EID: 84858342613     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2012.01.101     Document Type: Article
Times cited : (73)

References (30)
  • 1
    • 0002494352 scopus 로고
    • A review of food hydrolysis specific area
    • J. Adler-Nissen, Elsevier Applied Science Publishers Copenhagen, Denmark
    • J. Adler-Nissen A review of food hydrolysis specific area J. Adler-Nissen, Enzymatic hydrolysis of food proteins 1986 Elsevier Applied Science Publishers Copenhagen, Denmark 57 109
    • (1986) Enzymatic Hydrolysis of Food Proteins , pp. 57-109
    • Adler-Nissen, J.1
  • 2
    • 0025233926 scopus 로고
    • The comparative effects of recombinant hirudin (CGP 39393) and standard heparin on thrombus growth in rabbits
    • G. Agnelli, C. Pascucci, B. Cosmi, and G.G. Nenci The comparative effects of recombinant hirudin (CGP 39393) and standard heparin on thrombus growth in rabbits Thrombosis and Haemostasis 63 1990 204 207
    • (1990) Thrombosis and Haemostasis , vol.63 , pp. 204-207
    • Agnelli, G.1    Pascucci, C.2    Cosmi, B.3    Nenci, G.G.4
  • 3
    • 70249087270 scopus 로고    scopus 로고
    • BSF1 fibrinolytic enzyme from a marine bacterium Bacillus subtilis A26: Purification, biochemical and molecular characterization
    • R. Agrebi, A. Haddar, N. Hmidet, K. Jellouli, L. Manni, and M. Nasri BSF1 fibrinolytic enzyme from a marine bacterium Bacillus subtilis A26: Purification, biochemical and molecular characterization Process Biochemistry 44 2009 1252 1259
    • (2009) Process Biochemistry , vol.44 , pp. 1252-1259
    • Agrebi, R.1    Haddar, A.2    Hmidet, N.3    Jellouli, K.4    Manni, L.5    Nasri, M.6
  • 5
    • 77949802114 scopus 로고    scopus 로고
    • Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins
    • R. Balti, N. Nedjar-Arroume, D. Guillochon, and M. Nasri Analysis of novel angiotensin I-converting enzyme inhibitory peptides from enzymatic hydrolysates of cuttlefish (Sepia officinalis) muscle proteins Journal of Agricultural and Food Science 58 2010 3840 3846
    • (2010) Journal of Agricultural and Food Science , vol.58 , pp. 3840-3846
    • Balti, R.1    Nedjar-Arroume, N.2    Guillochon, D.3    Nasri, M.4
  • 6
    • 80155183346 scopus 로고    scopus 로고
    • Effect of protein hydrolysates from sardinelle (Sardinella aurita) on the oxidative status and blood lipid profile of cholesterol-fed rats
    • H. Ben Khaled, Z. Ghlissi, Y. Chtourou, A. Hakim, N. Ktari, and F. Makni-Ayedi Effect of protein hydrolysates from sardinelle (Sardinella aurita) on the oxidative status and blood lipid profile of cholesterol-fed rats Food Research International 45 2012 60 68
    • (2012) Food Research International , vol.45 , pp. 60-68
    • Ben Khaled, H.1    Ghlissi, Z.2    Chtourou, Y.3    Hakim, A.4    Ktari, N.5    Makni-Ayedi, F.6
  • 7
    • 1842434455 scopus 로고    scopus 로고
    • Optimization study for the production of an opioid-like preparation from bovine casein by mild acidic hydrolysis
    • L. Bitri Optimization study for the production of an opioid-like preparation from bovine casein by mild acidic hydrolysis International Dairy Journal 14 2004 535 539
    • (2004) International Dairy Journal , vol.14 , pp. 535-539
    • Bitri, L.1
  • 8
    • 60249083915 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates obtained by gastrointestinal proteases
    • A. Bougatef, M. Hajji, R. Balti, I. Lassoued, Y. Triki-Ellouz, and M. Nasri Antioxidant and free radical-scavenging activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates obtained by gastrointestinal proteases Food Chemistry 114 2009 1198 1205
    • (2009) Food Chemistry , vol.114 , pp. 1198-1205
    • Bougatef, A.1    Hajji, M.2    Balti, R.3    Lassoued, I.4    Triki-Ellouz, Y.5    Nasri, M.6
  • 9
    • 69349093252 scopus 로고    scopus 로고
    • Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins
    • A. Bougatef, N. Nedjar-Arroume, L. Manni, R. Ravallec, A. Barkia, and D. Guillochon Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins Food Chemistry 118 2010 559 565
    • (2010) Food Chemistry , vol.118 , pp. 559-565
    • Bougatef, A.1    Nedjar-Arroume, N.2    Manni, L.3    Ravallec, R.4    Barkia, A.5    Guillochon, D.6
  • 10
    • 0017335948 scopus 로고
    • Relationship between the anticoagulant and antithrombotic effects of heparin in experimental venous thrombosis
    • H.M. Chiu, J. Hirsh, W.L. Yung, E. Regoeczi, and M. Gent Relationship between the anticoagulant and antithrombotic effects of heparin in experimental venous thrombosis Blood 49 1977 171 184
    • (1977) Blood , vol.49 , pp. 171-184
    • Chiu, H.M.1    Hirsh, J.2    Yung, W.L.3    Regoeczi, E.4    Gent, M.5
  • 11
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood clotting
    • E.W. Davie, and O.D. Ratnoff Waterfall sequence for intrinsic blood clotting Science 145 1964 1310 1312
    • (1964) Science , vol.145 , pp. 1310-1312
    • Davie, E.W.1    Ratnoff, O.D.2
  • 12
    • 75749103376 scopus 로고    scopus 로고
    • Identification of an anticoagulant peptide that inhibits both fXIa and fVIIa/tissue factor from blood-feeding nematode Ancylostoma caninum
    • L. Deng, Q. He, T. Kang, H. Yin, X. Jin, and H. Li Identification of an anticoagulant peptide that inhibits both fXIa and fVIIa/tissue factor from blood-feeding nematode Ancylostoma caninum Biochemical and Biophysical Research Communications 392 2010 155 159
    • (2010) Biochemical and Biophysical Research Communications , vol.392 , pp. 155-159
    • Deng, L.1    He, Q.2    Kang, T.3    Yin, H.4    Jin, X.5    Li, H.6
  • 13
    • 36448957177 scopus 로고    scopus 로고
    • Antioxidant and biochemical properties of protein hydrolysates prepared from Silver carp (Hypophthalmichthys molitrix)
    • S. Dong, M. Zeng, D. Wang, Z. Liu, Y. Zhao, and H. Yang Antioxidant and biochemical properties of protein hydrolysates prepared from Silver carp (Hypophthalmichthys molitrix) Food Chemistry 107 2008 1485 1493
    • (2008) Food Chemistry , vol.107 , pp. 1485-1493
    • Dong, S.1    Zeng, M.2    Wang, D.3    Liu, Z.4    Zhao, Y.5    Yang, H.6
  • 14
    • 33847265270 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated Bacillus licheniformis NH1
    • N. El Hadj-Ali, R. Agrebi, B. Ghorbel-Frikha, A. Sellami-Kamoun, S. Kanoun, and M. Nasri Biochemical and molecular characterization of a detergent stable alkaline serine-protease from a newly isolated Bacillus licheniformis NH1 Enzyme and Microbial Technology 40 2007 515 523
    • (2007) Enzyme and Microbial Technology , vol.40 , pp. 515-523
    • El Hadj-Ali, N.1    Agrebi, R.2    Ghorbel-Frikha, B.3    Sellami-Kamoun, A.4    Kanoun, S.5    Nasri, M.6
  • 15
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • K. Erdman, B.W.Y. Cheung, and H. Schröder The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease Journal of Nutritional Biochemistry 19 2008 643 654
    • (2008) Journal of Nutritional Biochemistry , vol.19 , pp. 643-654
    • Erdman, K.1    Cheung, B.W.Y.2    Schröder, H.3
  • 16
    • 0005897660 scopus 로고    scopus 로고
    • FAO Food and Agriculture Organisation Rome, Italy
    • FAO (2004), Food and Agriculture Organisation. Fishery Statistics, Rome, Italy.
    • (2004) Fishery Statistics
  • 17
    • 77950299226 scopus 로고    scopus 로고
    • Application of statistical experimental design for optimization of keratinases production by Bacillus pumilus A1 grown on chicken feather and some biochemical properties
    • N. Fakhfakh-Zouari, A. Haddar, N. Hmidet, F. Frikha, and M. Nasri Application of statistical experimental design for optimization of keratinases production by Bacillus pumilus A1 grown on chicken feather and some biochemical properties Process Biochemistry 45 2010 617 626
    • (2010) Process Biochemistry , vol.45 , pp. 617-626
    • Fakhfakh-Zouari, N.1    Haddar, A.2    Hmidet, N.3    Frikha, F.4    Nasri, M.5
  • 18
    • 0027357826 scopus 로고
    • Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities
    • A.M. Fiat, D. Migliore-Samour, P. Jollés, L. Drouet, C. Collier, and J. Caen Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities Journal of Dairy Science 76 1993 301 310
    • (1993) Journal of Dairy Science , vol.76 , pp. 301-310
    • Fiat, A.M.1    Migliore-Samour, D.2    Jollés, P.3    Drouet, L.4    Collier, C.5    Caen, J.6
  • 19
    • 63449085549 scopus 로고    scopus 로고
    • Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: Purification, characterization and potential application as a laundry detergent additive
    • A. Haddar, R. Agrebi, A. Bougatef, A. Sellami-Kamoun, and M. Nasri Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: Purification, characterization and potential application as a laundry detergent additive Bioresource Technology 100 2009 3366 3373
    • (2009) Bioresource Technology , vol.100 , pp. 3366-3373
    • Haddar, A.1    Agrebi, R.2    Bougatef, A.3    Sellami-Kamoun, A.4    Nasri, M.5
  • 20
    • 67649336586 scopus 로고    scopus 로고
    • Isolation and characterization of an anticoagulant oligopeptide from blue mussel, Mytilus edulis
    • W.K. Jung, and S.K. Kim Isolation and characterization of an anticoagulant oligopeptide from blue mussel, Mytilus edulis Food Chemistry 117 2009 687 692
    • (2009) Food Chemistry , vol.117 , pp. 687-692
    • Jung, W.K.1    Kim, S.K.2
  • 21
    • 0027352759 scopus 로고
    • Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64
    • A.A. Kembhavi, A. Kulkarni, and A. Pant Salt-tolerant and thermostable alkaline protease from Bacillus subtilis NCIM No. 64 Applied Biochemistry and Biotechnology 38 1993 83 92
    • (1993) Applied Biochemistry and Biotechnology , vol.38 , pp. 83-92
    • Kembhavi, A.A.1    Kulkarni, A.2    Pant, A.3
  • 22
    • 0033822733 scopus 로고    scopus 로고
    • Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture
    • H.G. Kristinsson, and B.A. Rasco Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture Process Biochemistry 36 2000 131 139
    • (2000) Process Biochemistry , vol.36 , pp. 131-139
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 23
    • 37049044629 scopus 로고
    • An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier
    • R.G. Macfarlane An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier Nature 202 1964 498 499
    • (1964) Nature , vol.202 , pp. 498-499
    • MacFarlane, R.G.1
  • 24
    • 0034598319 scopus 로고    scopus 로고
    • Design, synthesis and structure-activity relationship of a series of arginine aldehyde factor Xa inhibitors. Part 1: Structures based on the (D)-Arg-Gly-Arg tripeptide sequence
    • C.K. Marlowe, U. Sinha, A.C. Gunn, and R.M. Scarborough Design, synthesis and structure-activity relationship of a series of arginine aldehyde factor Xa inhibitors. Part 1: structures based on the (D)-Arg-Gly-Arg tripeptide sequence Bioorganic and Medicinal Chemistry Letters 10 2000 13 16
    • (2000) Bioorganic and Medicinal Chemistry Letters , vol.10 , pp. 13-16
    • Marlowe, C.K.1    Sinha, U.2    Gunn, A.C.3    Scarborough, R.M.4
  • 25
    • 0038397187 scopus 로고    scopus 로고
    • Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects
    • H. Meisel, and R.J. FitzGerald Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects Current Pharmaceutical Design 9 2003 1289 1295
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1289-1295
    • Meisel, H.1    Fitzgerald, R.J.2
  • 26
    • 0032570258 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and specific family of factor Xa inhibitors via combinatorial chemistry
    • J.A. Ostrem, F. Al-Obeidi, P. Safar, A. Safarova, S.K. Stringer, and M. Patek Discovery of a novel, potent, and specific family of factor Xa inhibitors via combinatorial chemistry Biochemistry 37 1998 1053 1059
    • (1998) Biochemistry , vol.37 , pp. 1053-1059
    • Ostrem, J.A.1    Al-Obeidi, F.2    Safar, P.3    Safarova, A.4    Stringer, S.K.5    Patek, M.6
  • 28
    • 0036397541 scopus 로고    scopus 로고
    • Optimization of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology
    • C. Van der Ven, H. Gruppen, D.B.A. de Bont, and A.G.J. Voragen Optimization of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology International Dairy Journal 12 2002 813 820
    • (2002) International Dairy Journal , vol.12 , pp. 813-820
    • Van Der Ven, C.1    Gruppen, H.2    De Bont, D.B.A.3    Voragen, A.G.J.4
  • 29
    • 33947581389 scopus 로고    scopus 로고
    • A new method for determination of antithrombotic activity of egg white protein hydrolysate by microplate reader
    • W.G. Yang, Z. Wang, and S.Y. Xu A new method for determination of antithrombotic activity of egg white protein hydrolysate by microplate reader Chinese Chemical Letters 18 2007 449 451
    • (2007) Chinese Chemical Letters , vol.18 , pp. 449-451
    • Yang, W.G.1    Wang, Z.2    Xu, S.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.