Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Meredith Mudgett-Hunter"'
Autor:
Gina C. Jager, Leonard A. Herzenberg, Robert E. Bruccoleri, Meredith Mudgett-Hunter, David J. Panka, David R. Parks, Michael N. Margolies, Jiri Novotny, E Haber, J. F. Schildbach
Publikováno v:
Journal of Biological Chemistry. 266:4640-4647
Two spontaneous variants of the murine anti-digoxin antibody-producing hybridoma cell line 26-10 were isolated by two-color fluorescence-activated cell sorting on the basis of altered hapten binding. The variable region sequences of the antibodies pr
Publikováno v:
Molecular immunology. 30(4)
In vitro mutagenesis and immunoglobulin gene transfection were used to investigate the binding site of a monoclonal antibody, 2610, that binds to digoxin, a cardiac glycoside. A computer model was generated in order to select sites in the complementa
Autor:
Meredith Mudgett-Hunter, Frederick Warren, Edgar Haber, Hermann Oppermann, James S. Huston, Mei-Sheng Tai, John Mccartney
Publikováno v:
Methods in Enzymology ISBN: 9780121821043
Publisher Summary This chapter describes the minimal antibody binding site through the protein engineering of single-chain Fv analog and fusion proteins. In this approach, the genes encoding VH and VL domains of a given monoclonal antibody are connec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2315b9cef81fe78eb01eb97b141c576
https://doi.org/10.1016/0076-6879(91)03005-2
https://doi.org/10.1016/0076-6879(91)03005-2
Autor:
Meredith Mudgett-Hunter, Michael N. Margolies, Shi Chung Ng, Marlene A Jacobson, Edgar Haber, Richard I. Near, N W Hudson, Jonathan G. Seidman
Publikováno v:
Molecular immunology. 27(9)
We used immunoglobulin gene transfection to study the effect that substituting an homologous light (L) chain for a parental L chain has on antigen fine specificity and affinity. High-affinity monoclonal anti-digoxin antibodies 26-10 and 40-100 were s
Autor:
M S Tai, Jirí Novotný, D. Levinson, James S. Huston, R Crea, R J Ridge, Robert E. Bruccoleri, Edgar Haber, Michael N. Margolies, Meredith Mudgett-Hunter
Publikováno v:
Proceedings of the National Academy of Sciences. 85:5879-5883
A biosynthetic antibody binding site, which incorporated the variable domains of anti-digoxin monoclonal antibody 26-10 in a single polypeptide chain (Mr = 26,354), was produced in Escherichia coli by protein engineering. This variable region fragmen
Publikováno v:
The Journal of Immunology. 121:1132-1138
Latent group a allotypes were detected with a sensitive radioimmune inhibition assay. Sera, IgG preparations, and antibody fractions containing these allotypes inhibited the binding of insolubilized allotypic antisera to various radiolabeled antigens
Autor:
Michael N. Margolies, Jonathan Kaye, Ralph T. Kubo, Meredith Mudgett-Hunter, Richard I. Near, Michael L.B. Becker, Stephen M. Hedrick
Publikováno v:
Cell. 58:911-921
We have constructed a hybrid immunoglobulin (VDJH)-T cell receptor (C alpha) gene using the VDJH exon from a digoxin-specific antibody. This gene was used to make a line of transgenic mice. The hybrid VDJH-C alpha protein is expressed on a subset of
Autor:
Patricia K. Donahoe, Michael P. LaQuaglia, Meredith Mudgett-Hunter, Elizabeth C. Necklaws, Peter J. Hudson, David T. MacLaughlin
Publikováno v:
Endocrinology. 118:791-796
Müllerian inhibiting substance (MIS) is a 140,000-dalton glycoprotein responsible for regression of Müllerian ducts in a male embryo. It has recently been demonstrated that MIS inhibits the growth of tumors in vivo and in vitro. In this study, we h
Publikováno v:
Molecular Immunology. 22:477-488
High-affinity monoclonal antibodies specific for the cardiac glycoside digoxin provide a useful system for the study of structure-function relationships between antibody combining site and specific antigenic determinants. Fifteen high-affinity monocl
Autor:
Michael N. Margolies, David R. Parks, Lisa L. Peterson, Leonard A. Herzenberg, Meredith Mudgett-Hunter, David J. Panka, Edgar Haber
Publikováno v:
Proceedings of the National Academy of Sciences. 85:3080-3084
Rare spontaneous variants of the anti-digoxin antibody-producing hybridoma 40-150 (Ko = 5.4 x 10(9) M-1) were selected for altered antigen binding by two-color fluorescence-activated cell sorting. The parent antibody binds digoxin 890-fold greater th