Literature DB >> 8534837

A molecular model for the dependence of the osmotic pressure of bovine serum albumin upon concentration and pH.

A P Minton1.   

Abstract

Expressions derived from the effective hard particle model of Minton and Edelhoch (Biopolymers, 21 (1982) 451) account quantitatively for the combined data of Kanal et al. (Biophys. J., 66 (1994) 153) describing the osmotic pressure of bovine serum albumin as a function of protein concentration (< or = ca. 100 milligrams) and pH (3-8) in buffered 0.1 M NaCl. The best fit of the model yields a molar mass of 68360 and a pH-dependent value of the effective specific volume ranging from a minimum of -0.17 cm3/g at pH 4.6 (the isoelectric point) to maxima of 3.1 cm3/g at pH 3.0 and 2.2 cm3/g at pH 8.0. These values are shown to be consistent with the magnitude of known attractive and repulsive electrostatic interactions between proteins in solution.

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Year:  1995        PMID: 8534837     DOI: 10.1016/0301-4622(95)00046-z

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  17 in total

1.  Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model.

Authors:  A P Minton
Journal:  Biophys J       Date:  2000-01       Impact factor: 4.033

2.  Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: indefinite linear self-association of bacterial cell division protein FtsZ.

Authors:  G Rivas; J A Fernández; A P Minton
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-13       Impact factor: 11.205

3.  The glass transition behavior of the globular protein bovine serum albumin.

Authors:  Geoffrey J Brownsey; Timothy R Noel; Roger Parker; Stephen G Ring
Journal:  Biophys J       Date:  2003-12       Impact factor: 4.033

4.  The Influence of Crowding Conditions on the Thermodynamic Feasibility of Metabolic Pathways.

Authors:  Liliana Angeles-Martinez; Constantinos Theodoropoulos
Journal:  Biophys J       Date:  2015-12-01       Impact factor: 4.033

5.  Effects of macromolecular crowding on biochemical reaction equilibria: a molecular thermodynamic perspective.

Authors:  Zhongqiao Hu; Jianwen Jiang; Raj Rajagopalan
Journal:  Biophys J       Date:  2007-05-18       Impact factor: 4.033

6.  Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins.

Authors:  Cristina Fernández; Allen P Minton
Journal:  Biophys J       Date:  2009-03-04       Impact factor: 4.033

7.  Subtleties in control by metabolic channelling and enzyme organization.

Authors:  B N Kholodenko; J M Rohwer; M Cascante; H V Westerhoff
Journal:  Mol Cell Biochem       Date:  1998-07       Impact factor: 3.396

8.  Critical examination of the colloidal particle model of globular proteins.

Authors:  Prasad S Sarangapani; Steven D Hudson; Ronald L Jones; Jack F Douglas; Jai A Pathak
Journal:  Biophys J       Date:  2015-02-03       Impact factor: 4.033

Review 9.  Macromolecular Crowding In Vitro, In Vivo, and In Between.

Authors:  Germán Rivas; Allen P Minton
Journal:  Trends Biochem Sci       Date:  2016-09-23       Impact factor: 13.807

10.  Self crowding of globular proteins studied by small-angle x-ray scattering.

Authors:  David P Goldenberg; Brian Argyle
Journal:  Biophys J       Date:  2014-02-18       Impact factor: 4.033

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