Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Mich B. Hein"'
Publikováno v:
Annals of the New York Academy of Sciences
Autor:
Julian K.-C. Ma, Mich B. Hein
Publikováno v:
Trends in Biotechnology. 13:522-527
Plants are capable of synthesizing and assembling virtually every kind of antibody molecule, ranging from the smallest antigen-binding domains and fragments, to full-length, and even multimeric, antibodies. A number of plant hosts can be used, and be
Autor:
Julian K.-C. Ma, Mich B. Hein
Publikováno v:
Plant Physiology. 109:341-346
The original report of Hiatt (1989) initiated a wave of excitement at the realization that a complex mammalian protein such as immunoglobulin could be assembled within a plant cell. The general reaction was one of amazement, but interest in exploitin
Publikováno v:
Vaccine. 13:1051-1057
A modified tobacco mosaic virus (TMV) was used to direct the synthesis of TMV coat protein hybrids containing a 13 amino acid sequence of the murine zona pellucida ZP3 protein. This hybrid protein was found to be robust and accumulate to high concent
Autor:
Neil M. Cowen, Mich B. Hein
Publikováno v:
Plant Biotechnology 2002 and Beyond ISBN: 9789048162208
Green plants were an important historical source of medicines, and a primary source of humans’ first biopharmaceuticals. Because plants are the most efficient producers of protein on the planet, they are now being tapped as a production source for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c39386fb861f68d09aadfc575128d118
https://doi.org/10.1007/978-94-017-2679-5_10
https://doi.org/10.1007/978-94-017-2679-5_10
Autor:
Nicholas D. Vine, Mich B. Hein, Julian K.-C. Ma, Fei Wang, Alessandro Vitale, Emanuela Pedrazzini, Lorenzo Frigerio
Publikováno v:
Plant physiology (Online) 123 (2000): 1483–1494. doi:10.1104/pp.123.4.1483
info:cnr-pdr/source/autori:L. Frigerio, ND. Vine, E. Pedrazzini, MB. Hein, F. Wang, JK.-C. Ma and A. Vitale/titolo:Assembly, Secretion and Vacuolar Delivery of a Hybrid Immunoglobulin in Plants/doi:10.1104%2Fpp.123.4.1483/rivista:Plant physiology (Online)/anno:2000/pagina_da:1483/pagina_a:1494/intervallo_pagine:1483–1494/volume:123
info:cnr-pdr/source/autori:L. Frigerio, ND. Vine, E. Pedrazzini, MB. Hein, F. Wang, JK.-C. Ma and A. Vitale/titolo:Assembly, Secretion and Vacuolar Delivery of a Hybrid Immunoglobulin in Plants/doi:10.1104%2Fpp.123.4.1483/rivista:Plant physiology (Online)/anno:2000/pagina_da:1483/pagina_a:1494/intervallo_pagine:1483–1494/volume:123
Secretory immunoglobulin (Ig) A is a decameric Ig composed of four α-heavy chains, four light chains, a joining (J) chain, and a secretory component (SC). The heavy and light chains form two tetrameric Ig molecules that are joined by the J chain and
Autor:
Keith L. Wycoff, Mich B. Hein, Thomas Lehner, Ban Y. Hikmat, Nicholas D. Vine, Lloyd Yu, Julian K.-C. Ma, Daniel Chargelegue
Publikováno v:
Nature medicine. 4(5)
A functional comparison was made between a monoclonal secretory antibody generated in transgenic plants and its parent murine IgC antibody .The affinity constants of both antibodies for a Streptococcus mutans adhesion protein were similar. However th
Autor:
Julian K.-C. Ma, Mich B. Hein
Publikováno v:
Annals of the New York Academy of Sciences. 792
Plants have always been important in the pharmaceutical industry, and plant biotechnology now offers new applications. The use of heterologous expression systems for production of recombinant proteins including antibodies is no longer novel. Attentio
Publikováno v:
Genetic Engineering ISBN: 9781461365143
Antibody molecules, taken out of the context of the vertebrate immune system, are complex glycosylated proteins with high binding specificities for antigens. The variety of possible antigens is virtually limitless. Specific antibodies can be elicited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd85147741129a7e16d68ef3527c5b49
https://doi.org/10.1007/978-1-4615-3424-2_4
https://doi.org/10.1007/978-1-4615-3424-2_4
Publikováno v:
Biotechnology progress. 7(5)
Expression of cDNA constructs encoding full-length mouse immunoglobulin chains with their native leader sequences or fusion constructs substituting the native leader with a pre-pro sequence derived from Saccharomyces cerevisiae yielded blocked N-term