Literature DB >> 624346

Anomalous stability of insulin at very high pressure.

R B Murphy.   

Abstract

Insulin is unaffected by pressures of 48,000 b in the solid state at room temperature, as elucidated both by spectroscopic measurements and bioassay. Its compression curve is reversible. The presence of water does not alter this property. Of a number of other proteins investigated insulin appears to be unique with regard to its pressure stability. The relative rigidity of the molecule combined with its small size may account for some of these properties.

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Year:  1978        PMID: 624346     DOI: 10.1007/bf01944668

Source DB:  PubMed          Journal:  Experientia        ISSN: 0014-4754


  3 in total

1.  High hydrostatic pressure and enzymic activity: inhibition of multimeric enzymes by dissociation.

Authors:  J T Penniston
Journal:  Arch Biochem Biophys       Date:  1971-01       Impact factor: 4.013

2.  Pressure denaturation of metmyoglobin.

Authors:  A Zipp; W Kauzmann
Journal:  Biochemistry       Date:  1973-10-09       Impact factor: 3.162

3.  Insulin self-association. Spectrum changes and thermodynamics.

Authors:  R S Lord; F Gubensek; J A Rupley
Journal:  Biochemistry       Date:  1973-10-23       Impact factor: 3.162

  3 in total
  1 in total

1.  Probing insulin bioactivity in oral nanoparticles produced by ultrasonication-assisted emulsification/internal gelation.

Authors:  Marlene A Lopes; Bárbara Abrahim-Vieira; Claudia Oliveira; Pedro Fonte; Alessandra M T Souza; Tammy Lira; Joana A D Sequeira; Carlos R Rodrigues; Lúcio M Cabral; Bruno Sarmento; Raquel Seiça; Francisco Veiga; António J Ribeiro
Journal:  Int J Nanomedicine       Date:  2015-09-18
  1 in total

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