Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Michael Benjamin Mann"'
Autor:
Elizabeth A. Mendiaz, Thomas C. Boone, Michael Benjamin Mann, Linda O. Narhi, Keith Langley, Robert J. Toso, Yueh-Rong Hsu, Rashid Syed, Gay-May Wu, Hsieng Sen Lu, Jette Wypych
Publikováno v:
Journal of Biological Chemistry. 272:6406-6415
Soluble Escherichia coli-derived recombinant human stem cell factor (rhSCF) forms a non-covalently associated dimer. We have determined a dimer association constant (Ka) of 2-4 x 10(8) M-1, using sedimentation equilibrium and size exclusion chromatog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55482dd07293ff1d3338187e38789b18
https://doi.org/10.1074/jbc.272.10.6406
https://doi.org/10.1074/jbc.272.10.6406
Autor:
John C. Fieschko, Anthony D. Menjares, Michael Benjamin Mann, Karen C. Sitney, George Stearns, Craig Curless, Janice L. Stevenson, Larry B. Tsai, Marshall Davenport Snavely
Publikováno v:
Annals of the New York Academy of Sciences. 782:297-310
We have modified the tryptophanase promoter (PtnaA) for use as a temperature-independent promoter for the production of recombinant proteins. Although any protein will have a temperature range in which its expression is optimal, we find the tryptopha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c82b558dcf39d4fa3e71b0a40fb756a8
https://doi.org/10.1111/j.1749-6632.1996.tb40570.x
https://doi.org/10.1111/j.1749-6632.1996.tb40570.x
Autor:
Michael Benjamin Mann, Keith Langley, Hsieng Sen Lu, Wen Chang Chang, Elizabeth A. Mendiaz, Yueh-Rong Hsu
Publikováno v:
Biochemical Journal. 305:563-568
In its native state, recombinant human-stem-cell-factor (SCF) dimer can spontaneously and rapidly undergo hybridization when two different SCF dimer species are incubated together. SCF species differing in molecular charge, e.g., a wild-type SCF form
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::968b57401fbd9b31711007b3118cbef5
https://doi.org/10.1042/bj3050563
https://doi.org/10.1042/bj3050563
Publikováno v:
Biotechnology progress. 1(3)
A recombinant E. Coli K12 strain carrying a runaway-type plasmid with the gene for human alpha interferon analogue and capable of producing high levels of recombinant product [1], was grown in rich medium and compared to the host strain without plasm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b81683f1beca94709bff22382ad69074
https://pubmed.ncbi.nlm.nih.gov/20568163
https://pubmed.ncbi.nlm.nih.gov/20568163
Autor:
David T. Chow, Keith Langley, Hsieng Sen Lu, Michael Benjamin Mann, Shinichi Hara, Yueh Rong Hsu, Elizabeth A. Mendiaz, Wen Chang Chang
Publikováno v:
Biochemistry. 37(8)
During in vitro aging, deamidation of recombinant human stem cell factor produced in Escherichia. coli was detected by HPLC analysis and by the release of soluble ammonia. The deamidation rate is very slow in buffers at low pH or at low temperatures;
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33eea4abc8796da7a686754776fe3b6f
https://pubmed.ncbi.nlm.nih.gov/9485371
https://pubmed.ncbi.nlm.nih.gov/9485371
Autor:
Michael Benjamin Mann, Dennis Fenton, Larry B. Tsai, Michael L. Klein, Craig Curless, Por-Hsiung Lai, Bruce W. Altrock, Hsieng Sen Lu, William C. Kenney
Publikováno v:
Biochemical and Biophysical Research Communications. 156:733-739
Interleukin-2 produced from a recombinant E. coli was found to contain as much as 19% norleucine in place of methionine in a minimal medium fermentation. Medium supplementation experiments and use of a leucine-requiring mutant host strain indicated t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a3417476f12446f9b0c40e589b4610c
https://doi.org/10.1016/s0006-291x(88)80904-5
https://doi.org/10.1016/s0006-291x(88)80904-5
Publikováno v:
Biotechnology and bioengineering. 34(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b53bb31cd775afe80e5f0289612cd5bb
https://pubmed.ncbi.nlm.nih.gov/18588121
https://pubmed.ncbi.nlm.nih.gov/18588121