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Volumn 15, Issue 5, 2002, Pages 341-348

Dealing with intractable protein cores: Protein sequencing of the Mcg IgG and the Yvo IgM heavy chain variable domains

Author keywords

Antibody crystallography; Human monoclonal antibodies; Insoluble peptides; Protein sequencing

Indexed keywords

DODECYL SULFATE SODIUM; IMMUNOGLOBULIN G; IMMUNOGLOBULIN HEAVY CHAIN; MONOCLONAL ANTIBODY; BENCE JONES PROTEIN; IMMUNOGLOBULIN; IMMUNOGLOBULIN M; MYELOMA IMMUNOGLOBULINS; PARAPROTEIN;

EID: 0036761294     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/jmr.596     Document Type: Article
Times cited : (4)

References (22)
  • 1
    • 0021470578 scopus 로고
    • OMITMAP: An electron density map suitable for examination of errors in a macromolecular model
    • Bhat TN, Cohen GH. 1984. OMITMAP: An electron density map suitable for examination of errors in a macromolecular model. J. Appl. Crystallogr. 17: 244-248.
    • (1984) J. Appl. Crystallogr. , vol.17 , pp. 244-248
    • Bhat, T.N.1    Cohen, G.H.2
  • 2
    • 0000399682 scopus 로고
    • Cleavage of sperm whale myoglobin with cyanogen bromide
    • Edmundson AB. 1963. Cleavage of sperm whale myoglobin with cyanogen bromide. Nature 198: 354-357.
    • (1963) Nature , vol.198 , pp. 354-357
    • Edmundson, A.B.1
  • 3
    • 0001384132 scopus 로고
    • Amino-acid sequence of sperm whale myoglobin
    • Edmundson AB. 1965. Amino-acid sequence of sperm whale myoglobin. Nature 205: 883-887.
    • (1965) Nature , vol.205 , pp. 883-887
    • Edmundson, A.B.1
  • 4
    • 0000708184 scopus 로고
    • The amino-acid sequence of sperm whale myoglobin
    • Edmundson AB, Hirs CHW. 1961. The amino-acid sequence of sperm whale myoglobin. Nature 190: 663-672.
    • (1961) Nature , vol.190 , pp. 663-672
    • Edmundson, A.B.1    Hirs, C.H.W.2
  • 5
    • 85025313118 scopus 로고
    • On the structure of sperm whale myoglobin. I. The amino acid composition and terminal groups of the chromatographically purified protein
    • Edmundson AB, Hirs CHW. 1962a. On the structure of sperm whale myoglobin. I. The amino acid composition and terminal groups of the chromatographically purified protein. J. Mol. Biol. 5: 663-682.
    • (1962) J. Mol. Biol. , vol.5 , pp. 663-682
    • Edmundson, A.B.1    Hirs, C.H.W.2
  • 6
    • 85025334596 scopus 로고
    • On the structure of sperm whale myoglobin. II. The tryptic hydrolysis of the denatured protein
    • Edmundson AB, Hirs CHW. 1962b. On the structure of sperm whale myoglobin. II. The tryptic hydrolysis of the denatured protein. J. Mol. Biol. 5: 683-705.
    • (1962) J. Mol. Biol. , vol.5 , pp. 683-705
    • Edmundson, A.B.1    Hirs, C.H.W.2
  • 7
    • 0000854770 scopus 로고
    • On the structure of sperm whale myoglobin. III. The amino acid sequences of the smaller tryptic peptides containing aromatic residues
    • Edmundson AB, Hirs CHW. 1962c. On the structure of sperm whale myoglobin. III. The amino acid sequences of the smaller tryptic peptides containing aromatic residues. J. Mol. Biol. 5: 706-708.
    • (1962) J. Mol. Biol. , vol.5 , pp. 706-708
    • Edmundson, A.B.1    Hirs, C.H.W.2
  • 8
    • 0016721052 scopus 로고
    • Rotational allomerism and divergent evolution of domains in immunoglobulin light chains
    • Edmundson AB, Ely KR, Abola EE, Schiller M, Panagiotopoulos N. 1975. Rotational allomerism and divergent evolution of domains in immunoglobulin light chains. Biochemistry 14: 3953-3961.
    • (1975) Biochemistry , vol.14 , pp. 3953-3961
    • Edmundson, A.B.1    Ely, K.R.2    Abola, E.E.3    Schiller, M.4    Panagiotopoulos, N.5
  • 9
    • 84995032114 scopus 로고
    • Three-dimensional structure of the orthorhombic form of the Mcg Bence-Jones dimer
    • Yamamura Y, Tada T (eds)., Academic Press: Tokyo
    • Ely KR, Herron JN, Edmundson AB. 1983. Three-dimensional structure of the orthorhombic form of the Mcg Bence-Jones dimer. In Progress in Immunology V, Yamamura Y, Tada T (eds)., Academic Press: Tokyo; 61-66.
    • (1983) Progress in Immunology V , pp. 61-66
    • Ely, K.R.1    Herron, J.N.2    Edmundson, A.B.3
  • 10
    • 0016293306 scopus 로고
    • Primary structure of the Mcg λ chain
    • Fett JW, Deutsch HF. 1974. Primary structure of the Mcg λ chain. Biochemistry 13: 4102-4114.
    • (1974) Biochemistry , vol.13 , pp. 4102-4114
    • Fett, J.W.1    Deutsch, H.F.2
  • 11
    • 0015860266 scopus 로고
    • Chemical cleavage after tryptophan residues in proteins
    • Fontana A, Vita C, Toniolo C. 1973. Chemical cleavage after tryptophan residues in proteins. FEBS Lett. 32: 139-142.
    • (1973) FEBS Lett. , vol.32 , pp. 139-142
    • Fontana, A.1    Vita, C.2    Toniolo, C.3
  • 12
    • 13144267947 scopus 로고
    • The cyanogen bromide reaction
    • Gross E. 1967. The cyanogen bromide reaction. Meth. Enzymol. 11: 238-255.
    • (1967) Meth. Enzymol. , vol.11 , pp. 238-255
    • Gross, E.1
  • 13
    • 0027154092 scopus 로고
    • Three-dimensional structure of a human immunoglobulin with a hinge deletion
    • Guddat LW, Herron JN, Edmundson AB. 1993. Three-dimensional structure of a human immunoglobulin with a hinge deletion. Proc. Natl Acad. Sci. USA 90: 4271-4275.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4271-4275
    • Guddat, L.W.1    Herron, J.N.2    Edmundson, A.B.3
  • 14
    • 0000498985 scopus 로고
    • The nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate
    • Gundlach HG, Stein WH, Moore S. 1959. The nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate. J. Biol. Chem. 234: 1754-1760.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1754-1760
    • Gundlach, H.G.1    Stein, W.H.2    Moore, S.3
  • 17
    • 0031453303 scopus 로고    scopus 로고
    • Lactose synthesis in a Monotreme, the echidna (Tachyglossus aculeatus): Isolation and amino acid sequence of echidna alpha-lactalbumin
    • Messer M, Griffiths M, Rismiller PD, Shaw DC. 1997. Lactose synthesis in a Monotreme, the echidna (Tachyglossus aculeatus): Isolation and amino acid sequence of echidna alpha-lactalbumin. Comp. Biochem. Physiol. 118B: 403.
    • (1997) Comp. Biochem. Physiol. , vol.118 B , pp. 403
    • Messer, M.1    Griffiths, M.2    Rismiller, P.D.3    Shaw, D.C.4
  • 18
    • 0014736628 scopus 로고
    • Immunoglobulin M: Pentameric Fcμ fragments released by trypsin at higher temperatures
    • Plaut AG, Tomasi TB Jr. 1970. Immunoglobulin M: Pentameric Fcμ fragments released by trypsin at higher temperatures. Proc. Natl Acad. Sci. USA 65: 318-322.
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 318-322
    • Plaut, A.G.1    Tomasi T.B., Jr.2
  • 20
    • 84944817135 scopus 로고
    • The molecular replacement method
    • Rossmann MG. 1990. The molecular replacement method. Acta Crystallogr. A46: 73-82.
    • (1990) Acta Crystallogr. , vol.A46 , pp. 73-82
    • Rossmann, M.G.1
  • 21
    • 0015840644 scopus 로고
    • Structure of a λ-type Bence-Jones protein at 3.5 Å resolution
    • Schiffer M, Girling RL, Ely KR, Edmundson AB. 1973. Structure of a λ-type Bence-Jones protein at 3.5 Å resolution. Biochemistry 12: 4620-4631.
    • (1973) Biochemistry , vol.12 , pp. 4620-4631
    • Schiffer, M.1    Girling, R.L.2    Ely, K.R.3    Edmundson, A.B.4
  • 22
    • 0000708185 scopus 로고
    • Comparison between the amino-acid sequences of sperm whale myoglobin and of human myoglobin
    • Watson HC, Kendrew JC. 1961. Comparison between the amino-acid sequences of sperm whale myoglobin and of human myoglobin. Nature 190: 670-672.
    • (1961) Nature , vol.190 , pp. 670-672
    • Watson, H.C.1    Kendrew, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.