The use of light-scattering and turbidity measurements to study the kinetics of extensively aggregating proteins: αs-Casein

✍ Scribed by T. G. Parker; D. G. Dalgleish

• Publisher: Wiley (John Wiley & Sons)
• Year: 1977
• Tongue: English
• Weight: 862 KB
• Volume: 16
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1977.360161115

✦ Synopsis

Abstract

The Ca^2+^‐induced association of α~s~‐casein has been studied using the methods of stopped‐flow light‐scattering and stopped‐flow turbidity. The methods used are described, and the analysis of the results to give plots of M~w~ against time in the time‐scale 0–15 sec is demonstrated. The validity of the method is discussed, and it is shown to be applicable to the association kinetics of aggregating proteins whose molecular‐weight averages lie between 10^7^ and 10^9^. The method was used to study the association of bovine α~s~‐casein in the presence of Ca^2+^, and results obtained are briefly discussed in terms of possible association mechanisms, and a mechanism for the overall reaction of α~s~‐casein with Ca^2+^, and the subsequent precipitation of the caseinate is proposed.