Chemical and physico-chemical characterization of genetic variant D of bovine β-lactoglobulin

The recently discovered genetic variant of β-lactoglobulin, β-D, has been compared to those previously known. It has been shown that β-D varies from β-B by the substitution per subunit chain of a glutamine residue in β-D for glutamic acid in β-B. This conclusion has been verified by titration experi...

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Published inArchives of biochemistry and biophysics Vol. 129; no. 2; pp. 720 - 727
Main Authors Brignon, G., Ribadeau-Dumas, B., Garnier, J., Pantaloni, D., Guinand, S., Basch, Jay J., Timasheff, Serge N.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.02.1969
Subjects
Amino Acids - analysis
Animals
Autoanalysis
Cattle
Chemical Phenomena
Chemistry
Chymotrypsin
Electrophoresis
Genetic Variation
Hydrogen-Ion Concentration
Lactoglobulins - analysis
Molecular Biology
Optical Rotatory Dispersion
Peptides - analysis
Protein Hydrolysates
Spectrum Analysis
Ultracentrifugation
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Summary:The recently discovered genetic variant of β-lactoglobulin, β-D, has been compared to those previously known. It has been shown that β-D varies from β-B by the substitution per subunit chain of a glutamine residue in β-D for glutamic acid in β-B. This conclusion has been verified by titration experiments. Conformational studies have shown that the structure of β-D is indistinguishable from that of the other variants. Furthermore, β-D does not form the low temperature octamer, characteristic of the A variant, while it dissociates into subunits both at acid and alkaline pH, just as the other variants.
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ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(69)90233-1