HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Fox, K. K. Articles by Pallansch, M. J. Search for Related Content PubMed Articles by Fox, K. K. Articles by Pallansch, M. J.

Separation of ß-lactoglobulin from Other Milk Serum Proteins by Trichloroacetic Acid

Dairy Products Laboratory, Eastern Utilization Research and Development Division, USDA, Washington, D. C.

ABSTRACT

ß-Lactoglobulin can be easily separated from milk because it is the whey protein most resistant to precipitation by trichloroacetic acid. After removing casein from milk by acid precipitation, the residual whey is made up to contain 3% trichloroacetic acid. All proteins other than ß-lactoglobulin precipitate and can be filtered. The nitrate is concentrated by negative pressure dialysis, dialyzed free of low molecular weight materials, and lyophilized. The recovered ß-lactoglobulin had a specific rotation of –27.8 at 575 mµ, pH 4.75, an intrinsic viscosity of 4.1, and an electrophoretic mobility of –5.65 x 10^–5 cm²/v/sec in veronal buffer pH 8.6, 0.1 ionic strength. It is monophoretic in this buffer. These values agree closely with those obtained in similar analyses of a commercially available sample of 3 x crystallized ß-lactoglobulin prepared by salt fractionation.