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Reconstitution of w...
Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris.
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- Karlsson, Maria, 1985 (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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Fotiadis, Dimitrios (författare)
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- Sjövall Larsen, Sara (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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Johansson, Ingela (författare)
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- Hedfalk, Kristina, 1969 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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Engel, Andreas (författare)
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- Kjellbom, Per (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 2003
- 2003
- Engelska.
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Ingår i: FEBS Letters. - 1873-3468 .- 0014-5793. ; 537:1-3, s. 68-72
- Relaterad länk:
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http://dx.doi.org/10...
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https://research.cha...
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- The aquaporin PM28A is one of the major integral proteins in spinach leaf plasma membranes. Phosphorylation/dephosphorylation of Ser274 at the C-terminus and of Ser115 in the first cytoplasmic loop has been shown to regulate the water channel activity of PM28A when expressed in Xenopus oocytes. To understand the mechanisms of the phosphorylation-mediated gating of the channel the structure of PM28A is required. In a first step we have used the methylotrophic yeast Pichia pastoris for expression of the pm28a gene. The expressed protein has a molecular mass of 32462 Da as determined by matrix-assisted laser desorption ionization-mass spectrometry, forms tetramers as revealed by electron microscopy and is functionally active when reconstituted in proteoliposomes. PM28A was efficiently solubilized from urea- and alkali-stripped Pichia membranes by octyl-beta-D-thioglucopyranoside resulting in a final yield of 25 mg of purified protein per liter of cell culture.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- ultrastructure
- genetics
- physiology
- Oocytes
- Kinetics
- Spinacia oleracea
- DNA Primers
- isolation & purification
- physiology
- metabolism
- Animals
- genetics
- physiology
- Serine
- Spectrometry
- ultrastructure
- physiology
- Matrix-Assisted Laser Desorption-Ionization
- metabolism
- genetics
- Plant Proteins
- Aquaporins
- Mass
- physiology
- Xenopus laevis
- Proteolipids
- ultrastructure
- Recombinant Proteins
- Phosphoserine
- ultrastructure
- Ion Channels
- genetics
- Base Sequence
- Pichia
- Phosphorylation
- Female
- Aquaporin
- Overexpression
- Electron microscopy
- Mass spectrometry
- Reconstitution
- Pichia pastoris
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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