Literature DB >> 13897771

[Thermodynamic study of the reversible dissociation of beta-lactoglobulin B by pH greater than 5.5].

C GEORGES, S GUINAND, J TONNELAT.   

Abstract

Keywords:  GLOBULINS/chemistry; HYDROGEN-ION CONCENTRATION

Mesh：

Substances：

Year:  1962        PMID： 13897771     DOI： 10.1016/0006-3002(62)90664-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


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  3 in total

1.  Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5.

Authors:  Davide Mercadante; Laurence D Melton; Gillian E Norris; Trevor S Loo; Martin A K Williams; Renwick C J Dobson; Geoffrey B Jameson
Journal:  Biophys J       Date:  2012-07-17       Impact factor: 4.033

2.  The state of aggregation of red deer (Cervus elaphus L.) beta-lactoglobulin preparations near neutral pH.

Authors:  E I McDougall; J C Stewart
Journal:  Biochem J       Date:  1977-10-01       Impact factor: 3.857

3.  Estimation of the molecular weights of proteins by Sephadex gel-filtration.

Authors:  P Andrews
Journal:  Biochem J       Date:  1964-05       Impact factor: 3.766
  3 in total

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