Application of Polarization of Fluorescence Technique to Protein Studies. II. The Rotatory Properties of κ-Casein

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Abstract
The polarization of fluorescence technic was used to study the molecular size characteristics of K-casein. K-casein preparations yielded negative slopes for the reciprocal polarization vs temperature/viscosity graphs. This was caused by a temperature dependent association reaction between K-casein monomers and polymers making it impossible to calculate their apparent molecular volumes or relaxation times. The polarization of fluorescence properties of K-casein preparations was independent of the ionic strengths employed. The polarization of fluorescence properties were dependent upon addition of sucrose, pH and temperature.