Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Zen Kh"'
Autor:
Bengt Persson, Heinrich Jung, Zen Kh, H R Kaback, Thomas G. Consler, Kirsten Jung, G. Verner, Gilbert G. Privé
Publikováno v:
Proceedings of the National Academy of Sciences. 90:6934-6938
A simplified approach for purification of functional lactose permease from Escherichia coli is described that is based on the construction of chimeras between the permease and a 100-amino acid residue polypeptide containing the biotin acceptor domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d136e4e6cfd331c989686fb7a83912c5
https://doi.org/10.1073/pnas.90.15.6934
https://doi.org/10.1073/pnas.90.15.6934
Publikováno v:
Molecular and biochemical parasitology. 71(1)
Two mitochondrial proteins with molecular masses of 18 and 51 kDa were isolated from Leishmania tarentolae, and N-terminal amino-acid sequences were obtained. The cDNAs and genes encoding these proteins were cloned using RT-PCR. The proteins were ide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a98541f6ec850113e5397089916e3d4
https://pubmed.ncbi.nlm.nih.gov/7630384
https://pubmed.ncbi.nlm.nih.gov/7630384
Publikováno v:
Biochemistry. 34(10)
The lactose permease of Escherichia coli has 12 transmembrane hydrophobic domains in probable alpha-helical conformation connected by hydrophilic loops. Previous studies [Consler, T. G., Persson, B., et al. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 69
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a925cb3a2de6aefc1fbce351cf48085b
https://pubmed.ncbi.nlm.nih.gov/7880837
https://pubmed.ncbi.nlm.nih.gov/7880837
Publisher Summary This chapter discusses the helix packing in the C-terminal half of lactose permease. The lac permease of E. coli is providing a paradigm for secondary active transporters that transduce the free energy stored in electrochemical ion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38a5073fb031986c1a994771a1d245a3
https://doi.org/10.1016/s1874-5172(06)80010-6
https://doi.org/10.1016/s1874-5172(06)80010-6
Autor:
Stathis Frillingos, Weitzman C, Jianhua Wu, Gilbert G. Privé, M L Ujwal, Zen Kh, Kirsten Jung, H R Kaback, Heinrich Jung
Publikováno v:
Europe PubMed Central
The lactose permease (lac) of Escherichia coli is a paradigm for membrane transport proteins. Encoded by the lacY gene, the permease has been solubilized, purified to homogeneity, reconstituted into phospholipid vesicles and shown to catalyse the cou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb5da87e1523cd6985ecfd064becca0d
https://pubmed.ncbi.nlm.nih.gov/7823021
https://pubmed.ncbi.nlm.nih.gov/7823021
Publikováno v:
Biochemistry. 33(27)
The lactose permease of Escherichia coli is a membrane transport protein containing 12 transmembrane hydrophobic domains connected by hydrophilic loops. Coexpression of lacY gene fragments encoding contiguous polypeptides corresponding to the first a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd2d4bc84c307f7f1d2effdfd6eba577
https://pubmed.ncbi.nlm.nih.gov/8031753
https://pubmed.ncbi.nlm.nih.gov/8031753
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 50(Pt 4)
A novel strategy is presented for the crystallization of membrane proteins or other proteins with low solubility and/or stability. The method is illustrated with the lactose permease from Escherichia coli, in which a fusion is constructed between the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d587178a45b2c972a4a187747210de87
https://pubmed.ncbi.nlm.nih.gov/15299388
https://pubmed.ncbi.nlm.nih.gov/15299388
Publikováno v:
Europe PubMed Central
The lactose permease of Escherichia coli is a paradigm for polytopic membrane transport proteins that transduce free energy stored in an electrochemical ion gradient into work in the form of a concentration gradient. Although the permease consists of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17096fb757854660a7d0afd86ee0b19a
https://pubmed.ncbi.nlm.nih.gov/8144491
https://pubmed.ncbi.nlm.nih.gov/8144491
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