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Volumn 130, Issue 3, 2012, Pages 679-686

Biochemical characterisation of an aminopeptidase with highest preference for lysine from Japanese flounder skeletal muscle

Author keywords

Characterisation; Japanese flounder; Lysine aminopeptidase; Peptide mass fingerprinting; Purification

Indexed keywords

AMINO PEPTIDASE; AMMONIUM SULPHATE; CHARACTERISATION; FISH MUSCLES; FREE AMINO ACIDS; ISO-ELECTRIC POINTS; JAPANESE FLOUNDER; OPTIMUM TEMPERATURE; PEPTIDE MASS FINGERPRINTING; PURIFIED ENZYME; SKELETAL MUSCLE; TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 80052777040     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.07.109     Document Type: Article
Times cited : (9)

References (29)
  • 2
    • 21544469987 scopus 로고    scopus 로고
    • Degradation of myofibrillar proteins by a myofibril-bound serine proteinase in the skeletal muscle of crucian carp
    • M.J. Cao, X.J. Jiang, H.C. Zhong, Z.J. Zhang, and W.J. Su Degradation of myofibrillar proteins by a myofibril-bound serine proteinase in the skeletal muscle of crucian carp Food Chemistry 94 2006 7 13
    • (2006) Food Chemistry , vol.94 , pp. 7-13
    • Cao, M.J.1    Jiang, X.J.2    Zhong, H.C.3    Zhang, Z.J.4    Su, W.J.5
  • 4
    • 0024643644 scopus 로고
    • Purification and properties of an aminopeptidase from Alaska pollack, Theragra chalcogramma, roe
    • T.K. Chiou, T. Matsui, and S. Konosu Purification and properties of an aminopeptidase from Alaska pollack, Theragra chalcogramma, roe Journal of Biochemistry 105 1989 505 509
    • (1989) Journal of Biochemistry , vol.105 , pp. 505-509
    • Chiou, T.K.1    Matsui, T.2    Konosu, S.3
  • 6
    • 32544446610 scopus 로고    scopus 로고
    • Partial purification and characterization of an aminopeptidase from Eimeria tenella
    • DOI 10.1645/GE-554R.1
    • R.H. Fetterer, K.B. Miska, and R.C. Barfield Partial purification and characterization of an aminopeptidase from Eimeria tenella The Journal of Parasitology 91 2005 1280 1286 (Pubitemid 43235210)
    • (2005) Journal of Parasitology , vol.91 , Issue.6 , pp. 1280-1286
    • Fetterer, R.H.1    Miska, K.B.2    Barfield, R.C.3
  • 7
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: Properties and functions
    • DOI 10.1016/0168-6445(96)00020-4
    • T. Gonzales, and J. Robert-Baudouy Bacterial aminopeptidases: Properties and functions FEMS Microbiology Review 18 1996 319 344 (Pubitemid 26241885)
    • (1996) FEMS Microbiology Reviews , vol.18 , Issue.4 , pp. 319-344
    • Gonzales, T.1    Robert-Baudouy, J.2
  • 9
    • 56649123314 scopus 로고    scopus 로고
    • A new type of neuron-specific aminopeptidase NAP-2 in rat brain synaptosomes
    • M. Hui, and K.S. Hui A new type of neuron-specific aminopeptidase NAP-2 in rat brain synaptosomes Neurochemical International 53 2008 317 324
    • (2008) Neurochemical International , vol.53 , pp. 317-324
    • Hui, M.1    Hui, K.S.2
  • 10
    • 0037409612 scopus 로고    scopus 로고
    • In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): Effects of cathepsins B, D and L
    • DOI 10.1016/S0308-8146(02)00481-8, PII S0308814602004818
    • C. Ladrat, V. Verrez-Bagnis, J. Noël, and J. Fleurence In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L); effects of cathepsins B, D and L Food Chemistry 81 2003 517 525 (Pubitemid 36411761)
    • (2003) Food Chemistry , vol.81 , Issue.4 , pp. 517-525
    • Ladrat, C.1    Verrez-Bagnis, V.2    Noel, J.3    Fleurence, J.4
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of the bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 37549002565 scopus 로고    scopus 로고
    • Purification and characterization of a leucine aminopeptidase from the skeletal muscle of common carp (Cyprinus carpio)
    • B.X. Liu, X.L. Du, L.G. Zhou, K.J. Hara, W.J. Su, and M.J. Cao Purification and characterization of a leucine aminopeptidase from the skeletal muscle of common carp (Cyprinus carpio) Food Chemistry 108 2008 140 147
    • (2008) Food Chemistry , vol.108 , pp. 140-147
    • Liu, B.X.1    Du, X.L.2    Zhou, L.G.3    Hara, K.J.4    Su, W.J.5    Cao, M.J.6
  • 14
    • 0022364574 scopus 로고
    • Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain
    • DOI 10.1111/j.1471-4159.1985.tb04056.x
    • J.R. McDermott, D. Mantle, B. Lauffart, and A.M. Kidd Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain Journal of Neurochemistry 45 1985 752 759 (Pubitemid 16238536)
    • (1985) Journal of Neurochemistry , vol.45 , Issue.3 , pp. 752-759
    • McDermott, J.R.1    Mantle, D.2    Lauffart, B.3    Kidd, A.M.4
  • 15
    • 33646777832 scopus 로고    scopus 로고
    • --activated aminopeptidase from bovine skeletal muscle
    • DOI 10.1271/bbb.70.1110
    • - activated aminopeptidase from bovine skeletal muscle Bioscience Biotechnology and Biochemistry 70 2006 1110 1117 (Pubitemid 43765240)
    • (2006) Bioscience, Biotechnology and Biochemistry , vol.70 , Issue.5 , pp. 1110-1117
    • Migita, K.1    Nishimura, T.2
  • 16
    • 0042853211 scopus 로고    scopus 로고
    • Purification, characterization, and gene cloning of lysyl aminoeptidase from Streptococcus thermophilus YRC001
    • H. Motoshima, T. Shiraishi, F. Tsukasaki, and S. Kaminogawa Purification, characterization, and gene cloning of lysyl aminoeptidase from Streptococcus thermophilus YRC001 Bioscience Biotechnology and Biochemistry 67 2003 772 782 (Pubitemid 39251907)
    • (2003) Bioscience, Biotechnology and Biochemistry , vol.67 , Issue.4 , pp. 772-782
    • Motoshima, H.1    Shiraishi, T.2    Tsukasaki, F.3    Kaminogawa, S.4
  • 19
    • 14644414793 scopus 로고    scopus 로고
    • Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • DOI 10.1128/JB.187.6.2077-2083.2005
    • - containing, lysine-specific aminopeptidase from the Hyperthermophilic Archaeon Pyrococcus furiosus Journal of Bacteriology 187 2005 2077 2083 (Pubitemid 40316238)
    • (2005) Journal of Bacteriology , vol.187 , Issue.6 , pp. 2077-2083
    • Story, S.V.1    Shah, C.2    Jenney Jr., F.E.3    Adams, M.W.W.4
  • 20
    • 0027479013 scopus 로고
    • Aminopeptidase: Structure and function
    • A. Taylor Aminopeptidase: Structure and function FASEB Journal 7 1993 290 298
    • (1993) FASEB Journal , vol.7 , pp. 290-298
    • Taylor, A.1
  • 22
    • 0034120834 scopus 로고    scopus 로고
    • Contribution of muscle aminopeptidases to flavor development in dry-cured ham
    • DOI 10.1016/S0963-9969(00)00032-6, PII S0963996900000326
    • F. Toldrá, M.C. Aristoy, and M. Flores Contribution of muscle aminopeptidases to flavor development in dry-cured ham Food Research International 33 2000 181 185 (Pubitemid 30308694)
    • (2000) Food Research International , vol.33 , Issue.3-4 , pp. 181-185
    • Toldra, F.1    Aristoy, M.-C.2    Flores, M.3
  • 23
    • 0023739543 scopus 로고
    • Kinetics of substrate reaction during irreversible modification of enzyme activity
    • C.L. Tsou Kinetics of substrate reaction during irreversible modification of enzyme activity Advances in Enzymology and Related Areas of Molecular Biology 61 1988 381 436
    • (1988) Advances in Enzymology and Related Areas of Molecular Biology , vol.61 , pp. 381-436
    • Tsou, C.L.1
  • 26
    • 55549128960 scopus 로고    scopus 로고
    • Leucine aminopeptidase from red sea bream (Pagrus major) skeletal muscle: Purification, characterization, cellular location, and tissue distribution
    • G.P. Wu, M.J. Cao, Y. Chen, B.X. Liu, and W.J. Su Leucine aminopeptidase from red sea bream (Pagrus major) skeletal muscle: Purification, characterization, cellular location, and tissue distribution Journal of Agricultural and Food Chemistry 56 2008 9653 9660
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 9653-9660
    • Wu, G.P.1    Cao, M.J.2    Chen, Y.3    Liu, B.X.4    Su, W.J.5
  • 27
    • 74649085897 scopus 로고    scopus 로고
    • Purification and characterization of a collagenolytic serine proteinase from the skeletal muscle of red sea bream (Pagrus major)
    • G.P. Wu, S.H. Chen, G.M. Liu, L.J. Zhang, W.J. Su, and M.J. Cao Purification and characterization of a collagenolytic serine proteinase from the skeletal muscle of red sea bream (Pagrus major) Comparative Biochemistry and Physiology 155B 2010 281 287
    • (2010) Comparative Biochemistry and Physiology , vol.155 B , pp. 281-287
    • Wu, G.P.1    Chen, S.H.2    Liu, G.M.3    Zhang, L.J.4    Su, W.J.5    Cao, M.J.6
  • 29
    • 0031982551 scopus 로고    scopus 로고
    • Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing
    • S. Yasothornsrikul, T. Toneff, S.R. Hwang, and V.Y. Hook Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing Journal of Neurochemistry 70 1998 153 163 (Pubitemid 28020839)
    • (1998) Journal of Neurochemistry , vol.70 , Issue.1 , pp. 153-163
    • Yasothornsrikul, S.1    Toneff, T.2    Hwang, S.-R.3    Hook, V.Y.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.