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 Stanley, W. G. Articles by Whitnah, C. H. Search for Related Content PubMed Articles by Stanley, W. G. Articles by Whitnah, C. H.

Electrophoresis of Milk Proteins. I. Some Comparisons of Salt-Acid and Salt-Lyophilized Whey Fractions^1,2

Department of Chemistry, Kansas State College, Manhattan

ABSTRACT

1. Electrophoretic patterns were obtained for whey proteins. These proteins were prepared by two different procedures, namely, salt-acid and salt-lyophilized.
   
2. Six electrophoretically distinguishable components were split off by electrophoresis of these whey proteins.
   
3. No qualitative difference in whey proteins prepared by these methods was recognized.
   
4. The electrophoretic concentration of euglobulin by the salt-acid method was less than half the salt-lyophilized value, while for pseudoglobulin the salt-acid value was nearly double the salt-lyophilized.
   
5. The change of concentration could have been due to action of HC1 upon the immune lactoglobulins.
   
6. Relative percentages of component areas from salt-lyophilized proteins agreed qualitatively with those obtained by Smith and only for one component did areas from salt-acid proteins agree better with the data of Smith and of Deutsch.
   

¹ Contribution no. 399. Department of Chemistry, Kansas Agricultural Experiment Station, Manhattan.

² This paper contains part of the material presented by William G. Stanley in a thesis for the Master of Science Degree at Kansas State College. 1950.