메뉴 건너뛰기




Volumn 33, Issue 2, 2009, Pages 198-204

Isolation and partial characterisation of four novel plasma lectins from the American lobster Homarus americanus

Author keywords

Acute phase proteins; Acute phase response; C type lectin; Haemolymph; Immunity; Lobster health; Mannan binding protein; N acetylated glucosamine binding protein

Indexed keywords

AGAROSE; CARBOHYDRATE; DIMER; HOMODIMER; LECTIN; MONOMER; PROTEIN SUBUNIT; TRYPSIN;

EID: 54849413354     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2008.08.007     Document Type: Article
Times cited : (12)

References (46)
  • 1
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • Zelensky A.N., and Gready J.E. The C-type lectin-like domain superfamily. FEBS J 272 24 (2005) 6179-6217
    • (2005) FEBS J , vol.272 , Issue.24 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 2
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: a historical introduction and overview
    • Kilpatrick D.C. Animal lectins: a historical introduction and overview. Biochim Biophys Acta 1572 2-3 (2002) 187-197
    • (2002) Biochim Biophys Acta , vol.1572 , Issue.2-3 , pp. 187-197
    • Kilpatrick, D.C.1
  • 3
    • 0034694384 scopus 로고    scopus 로고
    • Lectins, as non-self-recognition factors, in crustaceans
    • Marques M., and Barracco M. Lectins, as non-self-recognition factors, in crustaceans. Aquaculture 191 (2000) 23-44
    • (2000) Aquaculture , vol.191 , pp. 23-44
    • Marques, M.1    Barracco, M.2
  • 4
    • 0036076660 scopus 로고    scopus 로고
    • Early events in crustacean innate immunity
    • Lee S.Y., and Soderhall K. Early events in crustacean innate immunity. Fish Shellfish Immunol 12 5 (2002) 421-437
    • (2002) Fish Shellfish Immunol , vol.12 , Issue.5 , pp. 421-437
    • Lee, S.Y.1    Soderhall, K.2
  • 6
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., and Lee B.L. Recent advances in the innate immunity of invertebrate animals. J Biochem Mol Biol 38 2 (2005) 128-150
    • (2005) J Biochem Mol Biol , vol.38 , Issue.2 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 7
    • 0043205805 scopus 로고    scopus 로고
    • Diverse lectin repertoires in tunicates mediate broad recognition and effector innate immune responses
    • Quesenberry M., Ahmed H., Elola M.T., O'Leary N., and Vasta G.R. Diverse lectin repertoires in tunicates mediate broad recognition and effector innate immune responses. Integr Comp Biol 43 (2003) 323-330
    • (2003) Integr Comp Biol , vol.43 , pp. 323-330
    • Quesenberry, M.1    Ahmed, H.2    Elola, M.T.3    O'Leary, N.4    Vasta, G.R.5
  • 8
    • 0001430320 scopus 로고
    • Lectins in the rock lobster Jasus novaehollandiae hemolymph
    • Imai T., Goto R., Kittaka J., and Kamiya H. Lectins in the rock lobster Jasus novaehollandiae hemolymph. Crustaceana 67 1 (1994) 121-130
    • (1994) Crustaceana , vol.67 , Issue.1 , pp. 121-130
    • Imai, T.1    Goto, R.2    Kittaka, J.3    Kamiya, H.4
  • 9
    • 15844399859 scopus 로고    scopus 로고
    • A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins
    • Armstrong P.B., Swarnakar S., Srimal S., Misquith S., Hahn E.A., Aimes R.T., et al. A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins. J Biol Chem 271 25 (1996) 14717-14721
    • (1996) J Biol Chem , vol.271 , Issue.25 , pp. 14717-14721
    • Armstrong, P.B.1    Swarnakar, S.2    Srimal, S.3    Misquith, S.4    Hahn, E.A.5    Aimes, R.T.6
  • 10
    • 0033618423 scopus 로고    scopus 로고
    • C-reactive protein and SAP-like pentraxin are both present in Limulus polyphemus haemolymph: crystal structure of Limulus SAP
    • Shrive A.K., Metcalfe A.M., Cartwright J.R., and Greenhough T.J. C-reactive protein and SAP-like pentraxin are both present in Limulus polyphemus haemolymph: crystal structure of Limulus SAP. J Mol Biol 290 5 (1999) 997-1008
    • (1999) J Mol Biol , vol.290 , Issue.5 , pp. 997-1008
    • Shrive, A.K.1    Metcalfe, A.M.2    Cartwright, J.R.3    Greenhough, T.J.4
  • 11
    • 0033199575 scopus 로고    scopus 로고
    • Functional and structural diversities of C-reactive proteins present in horseshoe crab hemolymph plasma
    • Iwaki D., Osaki T., Mizunoe Y., Wai S.N., Iwanaga S., and Kawabata S. Functional and structural diversities of C-reactive proteins present in horseshoe crab hemolymph plasma. Eur J Biochem 264 2 (1999) 314-326
    • (1999) Eur J Biochem , vol.264 , Issue.2 , pp. 314-326
    • Iwaki, D.1    Osaki, T.2    Mizunoe, Y.3    Wai, S.N.4    Iwanaga, S.5    Kawabata, S.6
  • 12
    • 0032992548 scopus 로고    scopus 로고
    • Role of lectins in the innate immunity of horseshoe crab
    • Kawabata S., and Iwanaga S. Role of lectins in the innate immunity of horseshoe crab. Dev Comp Immunol 23 4-5 (1999) 391-400
    • (1999) Dev Comp Immunol , vol.23 , Issue.4-5 , pp. 391-400
    • Kawabata, S.1    Iwanaga, S.2
  • 13
    • 33747818004 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of a putative C-type lectin (Fclectin) gene in Chinese shrimp Fenneropenaeus chinensis
    • Liu Y.C., Li F.H., Dong B., Wang B., Luan W., Zhang X.J., et al. Molecular cloning, characterization and expression analysis of a putative C-type lectin (Fclectin) gene in Chinese shrimp Fenneropenaeus chinensis. Mol Immunol 44 4 (2007) 598-607
    • (2007) Mol Immunol , vol.44 , Issue.4 , pp. 598-607
    • Liu, Y.C.1    Li, F.H.2    Dong, B.3    Wang, B.4    Luan, W.5    Zhang, X.J.6
  • 14
    • 33748852221 scopus 로고    scopus 로고
    • Cloning and characterization of a novel C-type lectin from Zhikong scallop Chlamys farreri
    • Wang H., Song L., Li C., Zhao J., Zhang H., Ni D., et al. Cloning and characterization of a novel C-type lectin from Zhikong scallop Chlamys farreri. Mol Immunol 44 5 (2007) 722-731
    • (2007) Mol Immunol , vol.44 , Issue.5 , pp. 722-731
    • Wang, H.1    Song, L.2    Li, C.3    Zhao, J.4    Zhang, H.5    Ni, D.6
  • 15
    • 33645883237 scopus 로고    scopus 로고
    • Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus
    • Nagoshi H., Inagawa H., Morii K., Harada H., Kohchi C., Nishizawa T., et al. Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus. Mol Immunol 43 13 (2006) 2061-2069
    • (2006) Mol Immunol , vol.43 , Issue.13 , pp. 2061-2069
    • Nagoshi, H.1    Inagawa, H.2    Morii, K.3    Harada, H.4    Kohchi, C.5    Nishizawa, T.6
  • 16
    • 34248195025 scopus 로고    scopus 로고
    • Molecular cloning of a C-type lectin (LvLT) from the shrimp Litopenaeus vannamei: early gene down-regulation after WSSV infection
    • Ma T.H., Tiu S.H., He J.G., and Chan S.M. Molecular cloning of a C-type lectin (LvLT) from the shrimp Litopenaeus vannamei: early gene down-regulation after WSSV infection. Fish Shellfish Immunol 23 2 (2007) 430-437
    • (2007) Fish Shellfish Immunol , vol.23 , Issue.2 , pp. 430-437
    • Ma, T.H.1    Tiu, S.H.2    He, J.G.3    Chan, S.M.4
  • 17
    • 0036634213 scopus 로고    scopus 로고
    • The lipopolysaccharide and beta-1,3-glucan binding protein gene is upregulated in white spot virus-infected shrimp (Penaeus stylirostris)
    • Roux M.M., Pain A., Klimpel K.R., and Dhar A.K. The lipopolysaccharide and beta-1,3-glucan binding protein gene is upregulated in white spot virus-infected shrimp (Penaeus stylirostris). J Virol 76 14 (2002) 7140-7149
    • (2002) J Virol , vol.76 , Issue.14 , pp. 7140-7149
    • Roux, M.M.1    Pain, A.2    Klimpel, K.R.3    Dhar, A.K.4
  • 18
    • 33846235195 scopus 로고    scopus 로고
    • Molecular cloning and mRNA expression of peptidoglycan recognition protein (PGRP) gene in bay scallop (Argopecten irradians, Lamarck 1819)
    • Ni D., Song L., Wu L., Chang Y., Yu Y., Qiu L., et al. Molecular cloning and mRNA expression of peptidoglycan recognition protein (PGRP) gene in bay scallop (Argopecten irradians, Lamarck 1819). Dev Comp Immunol 31 6 (2007) 548-558
    • (2007) Dev Comp Immunol , vol.31 , Issue.6 , pp. 548-558
    • Ni, D.1    Song, L.2    Wu, L.3    Chang, Y.4    Yu, Y.5    Qiu, L.6
  • 19
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • Gabay C., and Kushner I. Acute-phase proteins and other systemic responses to inflammation. N Engl J Med 340 6 (1999) 448-454
    • (1999) N Engl J Med , vol.340 , Issue.6 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 20
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway Jr. C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 54 Pt 1 (1989) 1-13
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 21
    • 0030434792 scopus 로고    scopus 로고
    • The interaction of C-reactive protein and serum amyloid P component with nuclear antigens
    • Du Clos T.W. The interaction of C-reactive protein and serum amyloid P component with nuclear antigens. Mol Biol Rep 23 3-4 (1996) 253-260
    • (1996) Mol Biol Rep , vol.23 , Issue.3-4 , pp. 253-260
    • Du Clos, T.W.1
  • 22
    • 0037374138 scopus 로고    scopus 로고
    • Recognition and clearance of apoptotic cells: a role for complement and pentraxins
    • Nauta A.J., Daha M.R., van K.C., and Roos A. Recognition and clearance of apoptotic cells: a role for complement and pentraxins. Trends Immunol 24 3 (2003) 148-154
    • (2003) Trends Immunol , vol.24 , Issue.3 , pp. 148-154
    • Nauta, A.J.1    Daha, M.R.2    van, K.C.3    Roos, A.4
  • 23
    • 1642545509 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins: on and off switches for innate immunity
    • Steiner H. Peptidoglycan recognition proteins: on and off switches for innate immunity. Immunol Rev 198 (2004) 83-96
    • (2004) Immunol Rev , vol.198 , pp. 83-96
    • Steiner, H.1
  • 24
    • 0015622273 scopus 로고
    • Partial characterization of a natural agglutinin in the hemolymph of the lobster, Homarus americanus
    • Cornick J.W., and Stewart J.E. Partial characterization of a natural agglutinin in the hemolymph of the lobster, Homarus americanus. J Invertebr Pathol 21 3 (1973) 255-262
    • (1973) J Invertebr Pathol , vol.21 , Issue.3 , pp. 255-262
    • Cornick, J.W.1    Stewart, J.E.2
  • 25
    • 0015954391 scopus 로고
    • Heterogeneity of lobster agglutinins. I. Purification and physiochemical characterization
    • Hall J.L., and Rowlands Jr. D.T. Heterogeneity of lobster agglutinins. I. Purification and physiochemical characterization. Biochemistry 13 4 (1974) 821-827
    • (1974) Biochemistry , vol.13 , Issue.4 , pp. 821-827
    • Hall, J.L.1    Rowlands Jr., D.T.2
  • 26
    • 0015954392 scopus 로고
    • Heterogeneity of lobster agglutinins. II. Specificity of agglutinin-erythrocyte binding
    • Hall J.L., and Rowlands Jr. D.T. Heterogeneity of lobster agglutinins. II. Specificity of agglutinin-erythrocyte binding. Biochemistry 13 4 (1974) 828-832
    • (1974) Biochemistry , vol.13 , Issue.4 , pp. 828-832
    • Hall, J.L.1    Rowlands Jr., D.T.2
  • 27
    • 0024999010 scopus 로고
    • Endogenously secreted IL-4 is required for mouse thymocytes to become cytotoxic. Human, but not mouse, IL-2 induces a functionally immature thymic subset to secrete IL-4 and become CTL
    • Stedman K.E., Justement L.B., and Campbell P.A. Endogenously secreted IL-4 is required for mouse thymocytes to become cytotoxic. Human, but not mouse, IL-2 induces a functionally immature thymic subset to secrete IL-4 and become CTL. Immunology 70 4 (1990) 478-484
    • (1990) Immunology , vol.70 , Issue.4 , pp. 478-484
    • Stedman, K.E.1    Justement, L.B.2    Campbell, P.A.3
  • 28
    • 0021117915 scopus 로고
    • Studies on the structure and carbohydrate binding properties of lobster agglutinin 1 (LAg1), a sialic acid-binding lectin
    • Abel C.A., Campbell P.A., VanderWall J., and Hartman A.L. Studies on the structure and carbohydrate binding properties of lobster agglutinin 1 (LAg1), a sialic acid-binding lectin. Prog Clin Biol Res 157 (1984) 103-114
    • (1984) Prog Clin Biol Res , vol.157 , pp. 103-114
    • Abel, C.A.1    Campbell, P.A.2    VanderWall, J.3    Hartman, A.L.4
  • 29
    • 0018083183 scopus 로고
    • An improved method for the isolation of lobster lectins
    • Hartman A.L., Campbell P.A., and Abel C.A. An improved method for the isolation of lobster lectins. Dev Comp Immunol 2 4 (1978) 617-625
    • (1978) Dev Comp Immunol , vol.2 , Issue.4 , pp. 617-625
    • Hartman, A.L.1    Campbell, P.A.2    Abel, C.A.3
  • 30
    • 85190490760 scopus 로고    scopus 로고
    • Gardner Pinfold Consulting Economists Ltd. Benchmarking study on Canadian lobster. Agriculture and Agri-Food Canada (AAFC); 2006. http://www.ats.agr.gc.ca/can/4217_e.htm.
    • Gardner Pinfold Consulting Economists Ltd. Benchmarking study on Canadian lobster. Agriculture and Agri-Food Canada (AAFC); 2006. http://www.ats.agr.gc.ca/can/4217_e.htm.
  • 31
    • 17744376367 scopus 로고    scopus 로고
    • Complexes of serum amyloid P component and DNA in serum from healthy individuals and systemic lupus erythematosus patients
    • Sørensen I.J., Nielsen E.H., Schrøder L., Voss A., Horváth L., and Svehag S. Complexes of serum amyloid P component and DNA in serum from healthy individuals and systemic lupus erythematosus patients. J Clin Immunol 20 6 (2000) 408-415
    • (2000) J Clin Immunol , vol.20 , Issue.6 , pp. 408-415
    • Sørensen, I.J.1    Nielsen, E.H.2    Schrøder, L.3    Voss, A.4    Horváth, L.5    Svehag, S.6
  • 32
    • 0023617937 scopus 로고
    • Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum
    • Pepys M.B., and Butler P.J. Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem Biophys Res Commun 148 1 (1987) 308-313
    • (1987) Biochem Biophys Res Commun , vol.148 , Issue.1 , pp. 308-313
    • Pepys, M.B.1    Butler, P.J.2
  • 33
    • 0032920138 scopus 로고    scopus 로고
    • High-level and effective production of human mannan-binding lectin (MBL) in Chinese hamster ovary (CHO) cells
    • Ohtani K., Suzuki Y., Eda S., Kawai T., Kase T., Keshi H., et al. High-level and effective production of human mannan-binding lectin (MBL) in Chinese hamster ovary (CHO) cells. J Immunol Methods 222 1-2 (1999) 135-144
    • (1999) J Immunol Methods , vol.222 , Issue.1-2 , pp. 135-144
    • Ohtani, K.1    Suzuki, Y.2    Eda, S.3    Kawai, T.4    Kase, T.5    Keshi, H.6
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. 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
  • 36
    • 2542423115 scopus 로고    scopus 로고
    • Mannan-binding lectin-a soluble pattern recognition molecule
    • Gadjeva M., Takahashi K., and Thiel S. Mannan-binding lectin-a soluble pattern recognition molecule. Mol Immunol 41 2-3 (2004) 113-121
    • (2004) Mol Immunol , vol.41 , Issue.2-3 , pp. 113-121
    • Gadjeva, M.1    Takahashi, K.2    Thiel, S.3
  • 37
    • 36248996465 scopus 로고    scopus 로고
    • Molecular and biological characterization of a mannan-binding lectin from the holothurian Apostichopus japonicus
    • Bulgakov A.A., Eliseikina M.G., Petrova I.Y., Nazarenko E.L., Kovalchuk S.N., Kozhemyako V.B., et al. Molecular and biological characterization of a mannan-binding lectin from the holothurian Apostichopus japonicus. Glycobiology 17 12 (2007) 1284-1298
    • (2007) Glycobiology , vol.17 , Issue.12 , pp. 1284-1298
    • Bulgakov, A.A.1    Eliseikina, M.G.2    Petrova, I.Y.3    Nazarenko, E.L.4    Kovalchuk, S.N.5    Kozhemyako, V.B.6
  • 38
    • 33846671423 scopus 로고    scopus 로고
    • Analysis of a cDNA-derived sequence of a novel mannose-binding lectin, codakine, from the tropical clam Codakia orbicularis
    • Gourdine J.P., and Smith-Ravin E.J. Analysis of a cDNA-derived sequence of a novel mannose-binding lectin, codakine, from the tropical clam Codakia orbicularis. Fish Shellfish Immunol 22 5 (2007) 498-509
    • (2007) Fish Shellfish Immunol , vol.22 , Issue.5 , pp. 498-509
    • Gourdine, J.P.1    Smith-Ravin, E.J.2
  • 39
    • 0033565726 scopus 로고    scopus 로고
    • Detection and characterization of a mannan-binding lectin from the mosquito, Anopheles stephensi (Liston)
    • Chen C., and Billingsley P.F. Detection and characterization of a mannan-binding lectin from the mosquito, Anopheles stephensi (Liston). Eur J Biochem 263 2 (1999) 360-366
    • (1999) Eur J Biochem , vol.263 , Issue.2 , pp. 360-366
    • Chen, C.1    Billingsley, P.F.2
  • 40
    • 33749147438 scopus 로고    scopus 로고
    • Characterization of a novel C-type lectin, Bombyx mori multibinding protein, from the B. mori hemolymph: mechanism of wide-range microorganism recognition and role in immunity
    • Watanabe A., Miyazawa S., Kitami M., Tabunoki H., Ueda K., and Sato R. Characterization of a novel C-type lectin, Bombyx mori multibinding protein, from the B. mori hemolymph: mechanism of wide-range microorganism recognition and role in immunity. J Immunol 177 7 (2006) 4594-4604
    • (2006) J Immunol , vol.177 , Issue.7 , pp. 4594-4604
    • Watanabe, A.1    Miyazawa, S.2    Kitami, M.3    Tabunoki, H.4    Ueda, K.5    Sato, R.6
  • 41
    • 4243869181 scopus 로고    scopus 로고
    • Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen
    • Gokudan S., Muta T., Tsuda R., Koori K., Kawahara T., Seki N., et al. Horseshoe crab acetyl group-recognizing lectins involved in innate immunity are structurally related to fibrinogen. Proc Natl Acad Sci USA 96 18 (1999) 10086-10091
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.18 , pp. 10086-10091
    • Gokudan, S.1    Muta, T.2    Tsuda, R.3    Koori, K.4    Kawahara, T.5    Seki, N.6
  • 42
    • 0019771211 scopus 로고
    • Isolation of a sialic acid-specific lobster lectin (LAg1) by affinity chromatography on Sepharose-colominic acid beads
    • VanderWall J., Campbell P.A., and Abel C.A. Isolation of a sialic acid-specific lobster lectin (LAg1) by affinity chromatography on Sepharose-colominic acid beads. Dev Comp Immunol 5 4 (1981) 679-683
    • (1981) Dev Comp Immunol , vol.5 , Issue.4 , pp. 679-683
    • VanderWall, J.1    Campbell, P.A.2    Abel, C.A.3
  • 43
    • 33744533045 scopus 로고    scopus 로고
    • Polysaccharide biological response modifiers
    • Leung M.Y., Liu C., Koon J.C., and Fung K.P. Polysaccharide biological response modifiers. Immunol Lett 105 2 (2006) 101-114
    • (2006) Immunol Lett , vol.105 , Issue.2 , pp. 101-114
    • Leung, M.Y.1    Liu, C.2    Koon, J.C.3    Fung, K.P.4
  • 44
    • 0033052588 scopus 로고    scopus 로고
    • C-type lectins and galectins mediate innate and adaptive immune functions: their roles in the complement activation pathway
    • Vasta G.R., Quesenberry M., Ahmed H., and O'Leary N. C-type lectins and galectins mediate innate and adaptive immune functions: their roles in the complement activation pathway. Dev Comp Immunol 23 4-5 (1999) 401-420
    • (1999) Dev Comp Immunol , vol.23 , Issue.4-5 , pp. 401-420
    • Vasta, G.R.1    Quesenberry, M.2    Ahmed, H.3    O'Leary, N.4
  • 45
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr Opin Immunol 14 1 (2002) 87-95
    • (2002) Curr Opin Immunol , vol.14 , Issue.1 , pp. 87-95
    • Iwanaga, S.1
  • 46
    • 0346305961 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in shrimp (Penaeus stylirostris) infected with White spot syndrome virus by cDNA microarrays
    • Dhar A.K., Dettori A., Roux M.M., Klimpel K.R., and Read B. Identification of differentially expressed genes in shrimp (Penaeus stylirostris) infected with White spot syndrome virus by cDNA microarrays. Arch Virol 148 12 (2003) 2381-2396
    • (2003) Arch Virol , vol.148 , Issue.12 , pp. 2381-2396
    • Dhar, A.K.1    Dettori, A.2    Roux, M.M.3    Klimpel, K.R.4    Read, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.