메뉴 건너뛰기




Volumn 23, Issue 1-3, 1997, Pages 151-159

Building high affinity human antibodies by altering the glycosylation on the light chain variable region in N-acetylglucosamine-supplemented hybridoma cultures

Author keywords

affinity; glucose; glycosylation; human antibody; N acetylglucosamine

Indexed keywords


EID: 0030974904     PISSN: 09209069     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1007980032042     Document Type: Article
Times cited : (22)

References (23)
  • 1
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C and Lesk AM (1987) Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol 196: 901-917.
    • (1987) J Mol Biol , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 2
    • 8244253535 scopus 로고
    • Source of the apparent carbohydrate content of bence-jones proteins
    • Clamp JR, Bernier GM and Putnam FW (1964) Source of the apparent carbohydrate content of bence-jones proteins. Biochim Biophys Acta 86: 149-155.
    • (1964) Biochim Biophys Acta , vol.86 , pp. 149-155
    • Clamp, J.R.1    Bernier, G.M.2    Putnam, F.W.3
  • 4
    • 0025840338 scopus 로고
    • The oligosaccharides of glycoproteins: Bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties
    • Goochee CF, Gramer MJ, Andersen DC, Bahr JB and Rasmussen JR (1991) The oligosaccharides of glycoproteins: bioprocess factors affecting oligosaccharide structure and their effect on glycoprotein properties. Biotechnol 9: 1347-1355.
    • (1991) Biotechnol , vol.9 , pp. 1347-1355
    • Goochee, C.F.1    Gramer, M.J.2    Andersen, D.C.3    Bahr, J.B.4    Rasmussen, J.R.5
  • 8
    • 0024207853 scopus 로고
    • Comparative study of the asparagine-linked sugar chains of natural human interferon-β1 and recombinant human interferon-β1 produced by three different mammalian cells
    • Kagawa Y, Takasaki S, Utsumi J, Hosoi K, Shimizu H, Kochibe N and Kobata A (1988) Comparative study of the asparagine-linked sugar chains of natural human interferon-β1 and recombinant human interferon-β1 produced by three different mammalian cells. J Biol Chem 263: 17508-17515.
    • (1988) J Biol Chem , vol.263 , pp. 17508-17515
    • Kagawa, Y.1    Takasaki, S.2    Utsumi, J.3    Hosoi, K.4    Shimizu, H.5    Kochibe, N.6    Kobata, A.7
  • 10
    • 0017405634 scopus 로고
    • Recognition of IgG by Fc receptor and complement: Effects of glycosidase digestion
    • Koide N, Nose M and Muramatsu T (1977) Recognition of IgG by Fc receptor and complement: Effects of glycosidase digestion. Biochem Biophys Res Commun 75: 838-844.
    • (1977) Biochem Biophys Res Commun , vol.75 , pp. 838-844
    • Koide, N.1    Nose, M.2    Muramatsu, T.3
  • 13
    • 0019404115 scopus 로고
    • Glucose starvation alters lipid linked oligosaccharide biosynthesis in chinese hamster ovary cells
    • Rearick JI, Chapman A and Kornfeld S (1981) Glucose starvation alters lipid linked oligosaccharide biosynthesis in chinese hamster ovary cells. J Biol Chem 256: 6255-6261.
    • (1981) J Biol Chem , vol.256 , pp. 6255-6261
    • Rearick, J.I.1    Chapman, A.2    Kornfeld, S.3
  • 14
    • 0014823629 scopus 로고
    • Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains
    • Sox HC Jr and Hood L (1970) Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains. Proc Natl Acad Sci USA 66: 975-982.
    • (1970) Proc Natl Acad Sci USA , vol.66 , pp. 975-982
    • Sox Jr., H.C.1    Hood, L.2
  • 15
    • 0018380713 scopus 로고
    • Glucose-dependent glcosylation of secretory glycoprotein in mouse myelooma cells
    • Stark NJ and Heath EC (1979) Glucose-dependent glcosylation of secretory glycoprotein in mouse myelooma cells. Arch Biochem Biophys 192: 599-609.
    • (1979) Arch Biochem Biophys , vol.192 , pp. 599-609
    • Stark, N.J.1    Heath, E.C.2
  • 16
    • 0027097020 scopus 로고
    • Generation of specificity-variant antibodies by alteration of carbohydrate in light chain of human monoclonal antibodies
    • Tachibana H, Shirahata S and Murakami H (1992) Generation of specificity-variant antibodies by alteration of carbohydrate in light chain of human monoclonal antibodies. Biochem Biophys Res Commun 189: 625-632.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 625-632
    • Tachibana, H.1    Shirahata, S.2    Murakami, H.3
  • 17
    • 0027501264 scopus 로고
    • Identification of hybrid-type carbohydrate chains on the light chain of human monoclonal antibody specific to lung adenocarcinoma
    • Tachibana H, Seki K and Murakami H (1993) Identification of hybrid-type carbohydrate chains on the light chain of human monoclonal antibody specific to lung adenocarcinoma. Biochem Biophys Acta 1182: 257-263.
    • (1993) Biochem Biophys Acta , vol.1182 , pp. 257-263
    • Tachibana, H.1    Seki, K.2    Murakami, H.3
  • 18
    • 0028721722 scopus 로고
    • Changes of monosaccharides availability of human hybridoma lead to alteration of biological properties of human monoclonal antibody
    • Tachibana H, Taniguchi K, Ushio Y, Teruya K, Osada K and Murakami H (1994) Changes of monosaccharides availability of human hybridoma lead to alteration of biological properties of human monoclonal antibody. Cytotechnology 16: 151-157.
    • (1994) Cytotechnology , vol.16 , pp. 151-157
    • Tachibana, H.1    Taniguchi, K.2    Ushio, Y.3    Teruya, K.4    Osada, K.5    Murakami, H.6
  • 19
    • 8244243086 scopus 로고
    • Generation of affinity-variant antibodies via the alteration of glycosylation in light chain effected by defined culture conditions of human hybridomas
    • Beuvery EC, Griffiths JB, Zeijlemaker WP (eds) Kluwer Academic Publishers, Dordrecht, Netherlands
    • Tachobana H, Kim J-Y, Murakami H (1995) Generation of affinity-variant antibodies via the alteration of glycosylation in light chain effected by defined culture conditions of human hybridomas. In: Animal Cell Technology: Developments towards the 21st. Century. Beuvery EC, Griffiths JB, Zeijlemaker WP (eds) pp 443-337. Kluwer Academic Publishers, Dordrecht, Netherlands.
    • (1995) Animal Cell Technology: Developments Towards the 21st. Century , pp. 443-1337
    • Tachobana, H.1    Kim, J.-Y.2    Murakami, H.3
  • 20
    • 0029866276 scopus 로고    scopus 로고
    • Modified antigen-binding of human antibodies with glycosylation variations of the light chains produced in sugar-limited human hybridoma cultures
    • Tachibana H, Kim J-Y, Taniguchi K, Ushio Y, Teruya K, Osada K, Inoue Y, Shirahata S and Murakami H (1996) Modified antigen-binding of human antibodies with glycosylation variations of the light chains produced in sugar-limited human hybridoma cultures. In Vitro Cell Dev Biol 32: 178-183.
    • (1996) In Vitro Cell Dev Biol , vol.32 , pp. 178-183
    • Tachibana, H.1    Kim, J.-Y.2    Taniguchi, K.3    Ushio, Y.4    Teruya, K.5    Osada, K.6    Inoue, Y.7    Shirahata, S.8    Murakami, H.9
  • 21
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T and Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 22
    • 0019276125 scopus 로고
    • Modification of oligosaccharide-lipid synthesis and protein glycosylation in glucose-deprived cells
    • Turco SJ (1980) Modification of oligosaccharide-lipid synthesis and protein glycosylation in glucose-deprived cells. Arch Biochem Biophys 205: 330-339.
    • (1980) Arch Biochem Biophys , vol.205 , pp. 330-339
    • Turco, S.J.1
  • 23


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.