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Journal of Dairy Science Vol. 83 No. 1 11-19
© 2000 by American Dairy Science Association ®
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Analysis of Major Caprine Milk Proteins by Reverse-Phase High-Performance Liquid Chromatography and Electrospray Ionization-Mass Spectrometry

A. J. Trujillo 1, I. Casals 2, and B. Guamis 1

1 Technologia del Aliments, Centre de Referència en Tecnologia dels Aliments (CeRTA), Facultat de Veterinària, Universitat Autònoma de Barcelona, 08193 Bellaterra, Spain
2 Serveis Científíco-Tècnics, Universitat de Barcelona, 08028 Barcelona, Spain

Major proteins from caprine milk were separated by preparative gel permeation and cation-exchange fast protein liquid chromatography and were characterized by flow injection analysis by electrospray ionization mass spectrometry. In addition, proteins from whole skim milk and whole casein were analyzed by coupling reverse-phase HPLC and electrospray ionization mass spectrometry by two different chromatographic methods. These methods successfully resolved the major caprine milk proteins and main casein variants. The experimental molecular masses of major milk proteins and variants were: 19,302 for kappa-CN 2P; 25,599 for alphas2-CN A-11P; 25,514 for alphas2-CN B-10P; 23,370 for alphas1-CN A-8P; 23,345 for alphas1-CN B-8P; 23,264 for alphas1-CN E-8P; 18,817 for alphas1-CN F-3P; 23,835 for ß-CN 6P; 18,181 for ß-LG; 14,180 for alpha-LA and 66,318 for serum albumin.

Key Words: caprine milk proteins • mass espectrometry • electrospray source

Submitted on March 8, 1999
Accepted on August 26, 1999






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