Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Elisabet Samuelsson"'
Publikováno v:
Nature Biotechnology. 14:751-755
We show that coexpression of a specific binding protein in Escherichia coli can significantly improve the relative yields of correctly folded human insulin-like growth factor I (IGF-I). A glutathione redox buffer was used during growth to allow forma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc7489c1a8116ecf76323cfdaac67391
https://doi.org/10.1038/nbt0696-751
https://doi.org/10.1038/nbt0696-751
Autor:
Elisabet Samuelsson, Mathias Uhlén
Publikováno v:
Annals of the New York Academy of Sciences. 782:486-494
A fusion partner, ZZ, derived from staphylococcal protein A, has earlier been shown facilitate the in vitro folding of human insulin-like growth factor I (IGF-I). Although no solubilizing agents were used, there was no problem with precipitation, eve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7e344bbe651c4fea2435c15c62d20a7
https://doi.org/10.1111/j.1749-6632.1996.tb40586.x
https://doi.org/10.1111/j.1749-6632.1996.tb40586.x
Autor:
Laurent Mignard, Mathias Uhlén, Stefan Ståhl, Maria Murby, Thien Ngoc Nguyen, Ultan F. Power, Hans Binz, Elisabet Samuelsson
Publikováno v:
European Journal of Biochemistry. 230:38-44
Site-directed mutagenesis has been employed to engineer the hydrophobic properties of a 101-amino-acid fragment from the human respiratory syncytial virus (RSV) major glycoprotein (G protein). When this protein was produced in Escherichia coli, more
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec7902beaa175cda555f099597d21ce
https://doi.org/10.1111/j.1432-1033.1995.0038i.x
https://doi.org/10.1111/j.1432-1033.1995.0038i.x
Autor:
Henrik Wadensten, Mathias Uhlén, E Holmgren, Maris Hartmanis, K Hall, M Tally, Elisabet Samuelsson, B Hammarberg, Tomas Moks
Publikováno v:
Journal of Biological Chemistry. 266:11058-11062
To investigate the biological role of variants of human insulin-like growth factor II (IGF-II), an extended form designated IGF-IIE21, with a molecular mass of 9.8 kDa, was produced in Escherichia coli as a stable and soluble secreted fusion protein.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab67d9663af3ebc5836c8440701e0bae
https://doi.org/10.1016/s0021-9258(18)99127-1
https://doi.org/10.1016/s0021-9258(18)99127-1
Publikováno v:
Journal of biotechnology. 48(3)
The potential for the development of an integrated process for production of human insulin and its C-peptide in Escherichia coli has been investigated. Human proinsulin was produced intracellularly in E. coli fused to two synthetic IgG-binding domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f50d9d02f7eadaf28c8f77649d4b41b
https://pubmed.ncbi.nlm.nih.gov/8862001
https://pubmed.ncbi.nlm.nih.gov/8862001
Publikováno v:
European journal of biochemistry. 236(2)
The kinetics for trypsin cleavage of different fusion proteins, consisting of human proinsulin and two IgG-binding domains (ZZ), were investigated. To achieve simultaneous removal of the fusion tag and processing of proinsulin to insulin and free C p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd0a76436da37036f7a234660ec12848
https://pubmed.ncbi.nlm.nih.gov/8612642
https://pubmed.ncbi.nlm.nih.gov/8612642
Publikováno v:
Biochemistry. 33(14)
We have previously shown that human insulin-like growth factor I (IGF-I), fused to ZZ (two domains derived from staphylococcal protein A), can be refolded at relatively high concentrations, without the use of solubilizing agents [Samuelsson, E., Wade
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::369110699cc2ec012de463c10720e2ad
https://pubmed.ncbi.nlm.nih.gov/8155636
https://pubmed.ncbi.nlm.nih.gov/8155636
Publisher Summary Insulin-like growth factor II (IGF-II) consists of 67 amino acid residues in a single chain. In analogy with IGF-I, there are 6 cysteine residues forming 3 disulfide bonds. The recombinant IGF-II was initially produced as a secreted
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a64ce93a289fd2834d7cbcbb29a1aa10
https://doi.org/10.1016/b978-0-12-058756-8.50038-9
https://doi.org/10.1016/b978-0-12-058756-8.50038-9
Publikováno v:
Bio/technology (Nature Publishing Company). 9(4)
We describe a new approach to refolding recombinant proteins in which an affinity fusion partner, consisting of two IgG-binding domains (ZZ) derived from staphylococcal protein A, is used to solubilize misfolded molecules before, during and after red
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4eb30dbe2d5aa0e257d89b274492cde5
https://pubmed.ncbi.nlm.nih.gov/1367009
https://pubmed.ncbi.nlm.nih.gov/1367009
Autor:
Charles N. Serhan, Elisabet Samuelsson, Elizabeth Goodman, Gerald Weissmann, Paul A. Anderson
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 77(3)
Multilamellar (MLV) and large unilamellar (LUV) lipid vesicles (liposomes) trap the metallochromic dye arsenazo III [2,7-bis(arsonophenylazo)-1,8-dihydroxynaphthalene-3,6-disulfonic acid ] in their aqueous compartments. When ionophore A23187 was prei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3de21b72449800c4a92d46b9bde988a0
https://pubmed.ncbi.nlm.nih.gov/6769114
https://pubmed.ncbi.nlm.nih.gov/6769114