Literature DB >> 3042460

An improved purification of lactose permease.

K Dornmair1.   

Abstract

The integral membrane protein lactose permease of Escherichia coli was purified to homogeneity in detergent micelles. No other proteins could be detected in the final product. The molar ratio of lactose permease to lipid was less than 0.2 in detergent solution, thus the preparation was essentially lipid-free. All molecules were functionally active as shown by substrate binding.

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Year:  1988        PMID: 3042460     DOI: 10.1016/0014-5793(88)81229-8

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


  2 in total

1.  Enhanced internal dynamics of a membrane transport protein during substrate translocation.

Authors:  K Doring; T Surrey; S Grünewald; E John; F Jähnig
Journal:  Protein Sci       Date:  2000-11       Impact factor: 6.725

2.  Characterization and functional reconstitution of a soluble form of the hydrophobic membrane protein lac permease from Escherichia coli.

Authors:  P D Roepe; H R Kaback
Journal:  Proc Natl Acad Sci U S A       Date:  1989-08       Impact factor: 11.205

  2 in total

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