메뉴 건너뛰기




Volumn 90, Issue 6, 2010, Pages 1034-1040

Purification and characterization of parvalbumins from silver carp (Hypophthalmichthy molitrix)

Author keywords

cDNA cloning; Characterization; Parvalbumin; Purification; Silver carp; Tricine SDS PAGE

Indexed keywords

ALLERGEN; FISH PROTEIN; ISOPROTEIN; MONOCLONAL ANTIBODY; PARVALBUMIN; POLYMER;

EID: 77949611833     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.3913     Document Type: Article
Times cited : (24)

References (30)
  • 2
    • 0014178556 scopus 로고
    • Studies of hypersensitivity to fish: Partial purification and crystallization of a major allergenic component of cod
    • Aas K and Jebsen JW, Studies of hypersensitivity to fish: partial purification and crystallization of a major allergenic component of cod. Int Arch Allergy Appl Immunol 32:1-20 (1967).
    • (1967) Int Arch Allergy Appl Immunol , vol.32 , pp. 1-20
    • Aas, K.1    Jebsen, J.W.2
  • 3
    • 28444477329 scopus 로고    scopus 로고
    • Allergy to fish parvalbumins: Studies on the cross-reactivity of allergens from 9 commonly consumed fish
    • Van Do T, Elsayed S, Florvaag E, Hordvik I and Endresen C, Allergy to fish parvalbumins: studies on the cross-reactivity of allergens from 9 commonly consumed fish. J Allergy Clin Immunol 116:1314-1320 (2005).
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 1314-1320
    • van Do, T.1    Elsayed, S.2    Florvaag, E.3    Hordvik, I.4    Endresen, C.5
  • 4
    • 33746879114 scopus 로고    scopus 로고
    • Detecting fish parvalbumin with commercial mouse monoclonal anti-frog parvalbumin IgG
    • Chen L, Hefle SL, Taylor SL, Swoboda I and Goodman RE, Detecting fish parvalbumin with commercial mouse monoclonal anti-frog parvalbumin IgG. J Agric Food Chem 54:5577-5582 (2006).
    • (2006) J Agric Food Chem , vol.54 , pp. 5577-5582
    • Chen, L.1    Hefle, S.L.2    Taylor, S.L.3    Swoboda, I.4    Goodman, R.E.5
  • 5
    • 33644911746 scopus 로고    scopus 로고
    • Comparison of allergenicity and allergens between fish white and dark muscles
    • Kobayashi A, Tanaka H, Hamada Y, Ishizaki S, Nagashima Y and Shiomi K, Comparison of allergenicity and allergens between fish white and dark muscles. Allergy 61:357-63 (2006).
    • (2006) Allergy , vol.61 , pp. 357-363
    • Kobayashi, A.1    Tanaka, H.2    Hamada, Y.3    Ishizaki, S.4    Nagashima, Y.5    Shiomi, K.6
  • 6
    • 16244384153 scopus 로고    scopus 로고
    • Missing parvalbumin: Implications in diagnostic testing for tuna allergy
    • Lim DL, Neo KH, Goh DL, Shek LP and Lee BW, Missing parvalbumin: implications in diagnostic testing for tuna allergy. J Allergy Clin Immunol 115:874-875 (2005).
    • (2005) J Allergy Clin Immunol , vol.115 , pp. 874-875
    • Lim, D.L.1    Neo, K.H.2    Goh, D.L.3    Shek, L.P.4    Lee, B.W.5
  • 7
    • 0036048803 scopus 로고    scopus 로고
    • A new oligomeric parvalbumin allergen of Atlantic cod (Gad mI) encoded by a gene distinct from that of Gad cI
    • Das Dores S, Chopin C, Villaume C, Fleurence J and Gueant JL, A new oligomeric parvalbumin allergen of Atlantic cod (Gad mI) encoded by a gene distinct from that of Gad cI. Allergy 57(Suppl 72):79-83 (2002).
    • (2002) Allergy , vol.57 , Issue.SUPPL. 72 , pp. 79-83
    • Das, D.S.1    Chopin, C.2    Villaume, C.3    Fleurence, J.4    Gueant, J.L.5
  • 8
    • 0031239640 scopus 로고    scopus 로고
    • Distribution of parvalbumin isotypes in adult snook and their potential applications as species-specific biomarkers
    • Ross C, Tilghman RW, Hartmann JX and Mari F, Distribution of parvalbumin isotypes in adult snook and their potential applications as species-specific biomarkers. J Fish Biol 51:561-572 (1997).
    • (1997) J Fish Biol , vol.51 , pp. 561-572
    • Ross, C.1    Tilghman, R.W.2    Hartmann, J.X.3    Mari, F.4
  • 9
    • 10344246575 scopus 로고    scopus 로고
    • Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M
    • Van Do T, Hordvik I, Endresen C and Elsayed S, Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M. Mol Immunol 42:345-353 (2005).
    • (2005) Mol Immunol , vol.42 , pp. 345-353
    • van Do, T.1    Hordvik, I.2    Endresen, C.3    Elsayed, S.4
  • 10
    • 0037831066 scopus 로고    scopus 로고
    • Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels
    • Hamada Y, Tanaka H, Ishizaki S, Ishida M, Nagashima Y and Shiomi K, Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels. Food Chem Toxicol 41:1149-1156 (2003).
    • (2003) Food Chem Toxicol , vol.41 , pp. 1149-1156
    • Hamada, Y.1    Tanaka, H.2    Ishizaki, S.3    Ishida, M.4    Nagashima, Y.5    Shiomi, K.6
  • 11
    • 68749098090 scopus 로고    scopus 로고
    • Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax
    • Beale JE, Jeebhay MF and Lopata AL, Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax. Mol Immunol 46:2985-2993 (2009).
    • (2009) Mol Immunol , vol.46 , pp. 2985-2993
    • Beale, J.E.1    Jeebhay, M.F.2    Lopata, A.L.3
  • 12
    • 0032722035 scopus 로고    scopus 로고
    • Expression and analysis of recombinant salmon parvalbumin, the major allergen in Atlantic salmon (Salmo salar)
    • Van Do T, Hordvik I, Endresen C and Elsayed S, Expression and analysis of recombinant salmon parvalbumin, the major allergen in Atlantic salmon (Salmo salar). Scand J Immunol 50:619-625 (1999).
    • (1999) Scand J Immunol , vol.50 , pp. 619-625
    • van Do, T.1    Hordvik, I.2    Endresen, C.3    Elsayed, S.4
  • 13
    • 4744356108 scopus 로고    scopus 로고
    • Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin
    • Hamada Y, Tanaka H, Sato A, Ishizaki S, Nagashima Y and Shiomi K, Expression and evaluation of IgE-binding capacity of recombinant Pacific mackerel parvalbumin. Allergol Int 53:271-278 (2004).
    • (2004) Allergol Int , vol.53 , pp. 271-278
    • Hamada, Y.1    Tanaka, H.2    Sato, A.3    Ishizaki, S.4    Nagashima, Y.5    Shiomi, K.6
  • 15
    • 0018800966 scopus 로고
    • Chicken parvalbumin: Comparison with parvalbumin-like protein and three other components (Mr = 8,000 to 13,000)
    • Heizmann CW and Strehler EE, Chicken parvalbumin: comparison with parvalbumin-like protein and three other components (Mr = 8,000 to 13,000). J Biol Chem 254:4296-4303 (1979).
    • (1979) J Biol Chem , vol.254 , pp. 4296-4303
    • Heizmann, C.W.1    Strehler, E.E.2
  • 16
    • 0017201271 scopus 로고
    • Parvalbumin from rabbit muscle: Isolation and primary structure
    • Capony JP, Pina C and Pechere JF, Parvalbumin from rabbit muscle: isolation and primary structure. Eur J Biochem 70:123-135 (1976).
    • (1976) Eur J Biochem , vol.70 , pp. 123-135
    • Capony, J.P.1    Pina, C.2    Pechere, J.F.3
  • 18
    • 0004844595 scopus 로고    scopus 로고
    • Purification, biochemical, and immunological characterization of a major food allergen: Different immuno globulin E recognition of the apo- and calcium-bound forms of carp parvalbumin
    • Bugajska-Schretter A, Grote M, Vangelista L, Valent P, Sperr WR, Rumpold H, et al, Purification, biochemical, and immunological characterization of a major food allergen: different immuno globulin E recognition of the apo- and calcium-bound forms of carp parvalbumin. Gut 46:661-669 (2000).
    • (2000) Gut , vol.46 , pp. 661-669
    • Bugajska-Schretter, A.1    Grote, M.2    Vangelista, L.3    Valent, P.4    Sperr, W.R.5    Rumpold, H.6    et al7
  • 19
    • 0036569405 scopus 로고    scopus 로고
    • Recombinant carp parvalbumin, the major cross-reactive fish allergen: A tool for diagnosis and therapy off is hallergy
    • Swoboda I, Bugajska-Schretter A, Verdino P, Keller W, Sperr WR, Valent P, et al, Recombinant carp parvalbumin, the major cross-reactive fish allergen: a tool for diagnosis and therapy off is hallergy. J Immunol 168:4576-4584 (2002).
    • (2002) J Immunol , vol.168 , pp. 4576-4584
    • Swoboda, I.1    Bugajska-Schretter, A.2    Verdino, P.3    Keller, W.4    Sperr, W.R.5    Valent, P.6    et al7
  • 20
    • 33847382030 scopus 로고    scopus 로고
    • Molecular cloning, expression and phylogenetic analyses of parvalbumin in tilapia, Oreochromis mossambicus
    • Lee SJ, Ju CC, Chu SL, Chien MS, Chan TH and Liao WL, Molecular cloning, expression and phylogenetic analyses of parvalbumin in tilapia, Oreochromis mossambicus. J Exp Zool A Ecol Genet Physiol 307:51-61 (2007).
    • (2007) J Exp Zool a Ecol Genet Physiol , vol.307 , pp. 51-61
    • Lee, S.J.1    Ju, C.C.2    Chu, S.L.3    Chien, M.S.4    Chan, T.H.5    Liao, W.L.6
  • 21
    • 67651156164 scopus 로고    scopus 로고
    • Comparison of allergenic properties of salmon (Oncorhynchus nerka) between landlocked and anadromous species
    • Kondo Y, Ahn J, Komatsubara R, Terada A, Yasuda T, Tsuge I, et al, Comparison of allergenic properties of salmon (Oncorhynchus nerka) between landlocked and anadromous species. Allergol Int 58:295-299 (2009).
    • (2009) Allergol Int , vol.58 , pp. 295-299
    • Kondo, Y.1    Ahn, J.2    Komatsubara, R.3    Terada, A.4    Yasuda, T.5    Tsuge, I.6    et al7
  • 23
    • 77949638912 scopus 로고    scopus 로고
    • Analysis of specific allergens IgE inbronchial asthma children in Wuhan district
    • (in Chinese)
    • Wu QW, Cai PC, Chen ZZ, Wu XH, Kong LL, Hu LH, et al, Analysis of specific allergens IgE inbronchial asthma children in Wuhan district. J Clin Hematology 22: 65-67 (2009). (in Chinese).
    • (2009) J Clin Hematology , vol.22 , pp. 65-67
    • Wu, Q.W.1    Cai, P.C.2    Chen, Z.Z.3    Wu, X.H.4    Kong, L.L.5    Hu, L.H.6    et al7
  • 24
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H, Tricine-SDS-PAGE. Nat Protoc 1:16-22 (2006).
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 25
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T and Gordon J, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354 (1979).
    • (1979) Proc Natl Acad Sci Usa , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0030816653 scopus 로고    scopus 로고
    • Food hypersensitivity and allergic disease: A selective review
    • Chandra RK, Food hypersensitivity and allergic disease: a selective review. Am J Clin Nutr 66: 526S-529S (1997).
    • (1997) Am J Clin Nutr , vol.66
    • Chandra, R.K.1
  • 28
    • 41449094497 scopus 로고    scopus 로고
    • Allergens are distributed into few protein families and possess a restricted number of biochemical functions
    • Radauer C, Bublin M, Wagner S, Mari A and Breiteneder H, Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol 121:847-852 (2008).
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 847-852
    • Radauer, C.1    Bublin, M.2    Wagner, S.3    Mari, A.4    Breiteneder, H.5
  • 29
    • 0031758168 scopus 로고    scopus 로고
    • Protein modification by thermal processing
    • Davis PJ and Williams SC, Protein modification by thermal processing. Allergy 53:102-105 (1998).
    • (1998) Allergy , vol.53 , pp. 102-105
    • Davis, P.J.1    Williams, S.C.2
  • 30
    • 33846229702 scopus 로고    scopus 로고
    • Biochemical characterization and thermostable capacity of parvalbumin: The major fish-food allergens
    • Arif SH, Jabeen M and Hasnain A, Biochemical characterization and thermostable capacity of parvalbumin: the major fish-food allergens. J Food Biochem 31:121-137 (2007).
    • (2007) J Food Biochem , vol.31 , pp. 121-137
    • Arif, S.H.1    Jabeen, M.2    Hasnain, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.