Literature DB >> 2873058

Thermostability of membrane systems in organic solvents.

G Ayala, M T de Gómez-Puyou, A Gómez-Puyou, A Darszon.   

Abstract

Two multisubunit enzymes of the inner mitochondrial membrane, cytochrome oxidase and the H+-ATPase may be transferred into highly apolar solvents as protein-lipid complexes. At 70 degrees C and an initial water concentration of 13 microliters per ml organic solvent (toluene), the half-life of the ATPase was approx. 11 h, whereas that of cytochrome oxidase was about 100 s. Thermostability of cytochrome oxidase could be increased more than 100-times by decreasing the water concentration to 3 microliters per ml toluene. At this latter concentration of water the half-life of the ATPase at 90, 80 and 70 degrees C was 5, 48 and 96 h, respectively.

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Year:  1986        PMID: 2873058     DOI: 10.1016/0014-5793(86)81432-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

Review 1.  Proton-coupled electron transfer.

Authors:  My Hang V Huynh; Thomas J Meyer
Journal:  Chem Rev       Date:  2007-11       Impact factor: 60.622

2.  Biocatalysis in nonaqueous media. Patents and literature.

Authors:  J S Dordick
Journal:  Appl Biochem Biotechnol       Date:  1988-10       Impact factor: 2.926

3.  Thermostable cellobiohydrolase from the thermophilic eubacterium Thermotoga sp. strain FjSS3-B.1. Purification and properties.

Authors:  L D Ruttersmith; R M Daniel
Journal:  Biochem J       Date:  1991-08-01       Impact factor: 3.857

  3 in total

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