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Molecular weights of subunit components of bovine casein micelles

Published online by Cambridge University Press:  01 June 2009

Tomotada Ono  and
Toshio Takagi
Tomotada Ono
Affiliation:
Department of Agricultural Chemistry, Iwate University, Morioka 020, Japan
Toshio Takagi
Affiliation:
Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan
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Summary

Using either Sephacryl S-300 or TSK-G4000SW gel chromatography, the larger of the two major components of bovine casein micelles (F2) was eluted at the same retention time irrespective of sample concentration and column temperature. Its mol. wt was estimated to be 500K by examination of the eluate from a TSK-gel G4000SW column using a low-angle laser light-scattering photometer and a precision differential refractometer. With the second component (F3), retention time in Sephacryl gel chromatography was significantly affected by both sample concentra-tion and volume applied. Limiting retention times for F3 could be obtained by extrapolation of these two parameters to higher and lower values, and corresponded to those of water-soluble protein with mol. wt 200K and 100K respectively. Approach to sedimentation equilibrium technique at the above limiting sample concentrations gave values of F3 consistent with the above molecular weight. Sephacryl gel chromatography at either low sample concentration or low column temperature resulted in a new component being eluted at a position of mol. wt 25K

Type
Original Articles
Information
Journal of Dairy Research , Volume 53 , Issue 4 , November 1986 , pp. 547 - 555
Copyright
Copyright © Proprietors of Journal of Dairy Research 1986

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References

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