Literature DB >> 1366838

Peptide hydrophobicity and partitioning in poly(ethylene glycol)/magnesium sulfate aqueous two-phase systems.

M A Eiteman1, J L Gainer.   

Abstract

Several amino acids and peptides were partitioned in poly(ethylene glycol) (PEG)/magnesium sulfate (MgSO4) aqueous two-phase systems. The partition coefficients measured for amino acids and peptides were proportional to the difference in PEG concentration between the phases. The partitioning data were used to calculate the relative hydrophobicities of individual amino acids, which were then used to estimate the hydrophobicities of peptides. The partition coefficients of several dipeptides were predicted from these estimated hydrophobicities. A series of peptide fragments that compose the pentapeptide leucine enkephalin was also partitioned in the PEG/MgSO4 system. Again, the partitioning depended upon the hydrophobicities of the individual exposed amino acids.

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Year:  1990        PMID: 1366838     DOI: 10.1021/bp00006a011

Source DB:  PubMed          Journal:  Biotechnol Prog        ISSN: 1520-6033


  2 in total

1.  Interactions of macromolecular crowding agents and cosolutes with small-molecule substrates: effect on horseradish peroxidase activity with two different substrates.

Authors:  William M Aumiller; Bradley W Davis; Emmanuel Hatzakis; Christine D Keating
Journal:  J Phys Chem B       Date:  2014-08-26       Impact factor: 2.991

2.  Coupled enzyme reactions performed in heterogeneous reaction media: experiments and modeling for glucose oxidase and horseradish peroxidase in a PEG/citrate aqueous two-phase system.

Authors:  William M Aumiller; Bradley W Davis; Negar Hashemian; Costas Maranas; Antonios Armaou; Christine D Keating
Journal:  J Phys Chem B       Date:  2014-02-21       Impact factor: 2.991

  2 in total

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