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

Biophysical Journal

Volumn 103, Issue 2, 2012, Pages 303-312

  Mercadante, Davide ^a,b   Melton, Laurence D ^a,b   Norris, Gillian E ^a   Loo, Trevor S ^a   Williams, Martin A K ^a   Dobson, Renwick C J ^c,d   Jameson, Geoffrey B ^a  

^a MASSEY UNIVERSITY   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

^c UNIVERSITY OF MELBOURNE   (Australia)

^d UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

LACTOGLOBULIN;

ANIMAL; ARTICLE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; MOLECULAR WEIGHT; PH; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; STATIC ELECTRICITY; THERMODYNAMICS; ULTRACENTRIFUGATION;

ANIMALS; CATTLE; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOGLOBULINS; MODELS, MOLECULAR; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; STATIC ELECTRICITY; THERMODYNAMICS; ULTRACENTRIFUGATION;

BOVINAE;

EID: 84864744643     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.05.041     Document Type: Article

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