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Articles citing this paper

On the Dissociation of Bovine ,b-Lactoglobulins A, B, and C Near Ph 7

HA Mckenzie and WH Sawyer
25(5) pp.949 - 962


6 articles found in Crossref database.

The emulsifying properties of β-lactoglobulin genetic variants A, B and C
R. Euston Stephen, L. Hirst Robyn, P. Hill Jeremy
Colloids and Surfaces B: Biointerfaces. 1999 12(3-6). p.193
Functional implications of structural differences between variants A and B of bovine β‐lactoglobulin
Qin Bin Y., Jameson Geoffrey B., Bewley Maria C., Baker Edward N., Creamer Lawrence K.
Protein Science. 1999 8(1). p.75
Self-association of β-lactoglobulin c in acetate buffers
Sarquis Jerry L., Adams E.T.
Biophysical Chemistry. 1976 4(2). p.181
Sedimentation equilibrium in reacting systems. VII. The temperature-dependent self-association of β-lactoglobulin A at pH 2.46
Tang Lih-Heng, Adams E.T.
Archives of Biochemistry and Biophysics. 1973 157(2). p.520
The temperature-dependent self-association of β-lactoglobulin C in glycine buffers
Sarquis Jerry L., Adams E.T.
Archives of Biochemistry and Biophysics. 1974 163(2). p.442
Bovine β-Lactoglobulin Is Dimeric Under Imitative Physiological Conditions: Dissociation Equilibrium and Rate Constants over the pH Range of 2.5–7.5
Mercadante Davide, Melton Laurence D., Norris Gillian E., Loo Trevor S., Williams Martin A.K., Dobson Renwick C.J., Jameson Geoffrey B.
Biophysical Journal. 2012 103(2). p.303
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