Literature DB >> 4738380

Sedimentation equilibrium in reacting systems. VII. The temperature-dependent self-association of beta-lactoglobulin A at pH 2.46.

L H Tang, E T Adams.   

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Year:  1973        PMID： 4738380     DOI： 10.1016/0003-9861(73)90671-1

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


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  3 in total

1.  Protein self-association in solution: the bovine beta -lactoglobulin dimer and octamer.

Authors:  Michael Gottschalk; Hanna Nilsson; Helena Roos; Bertil Halle
Journal:  Protein Sci       Date:  2003-11       Impact factor: 6.725

2.  A high-throughput method for detection of protein self-association and second virial coefficient using size-exclusion chromatography through simultaneous measurement of concentration and scattered light intensity.

Authors:  Harminder Bajaj; Vikas K Sharma; Devendra S Kalonia
Journal:  Pharm Res       Date:  2007-06-19       Impact factor: 4.200

3.  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
  3 in total

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