Analysis of major caprine milk proteins by reverse-phase high-performance liquid chromatography and electrospray ionization-mass spectrometry

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    Resum

    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 κ-CN 2P; 25,599 for αs2-CN A-11P; 25,514 for αs2-CN B-10P; 23,370 for αs1-CN A-8P; 23,345 for γs1-CN B-8P; 23,264 for αs1-CN E-8P; 18,817 for αs1-CN F-3P; 23,835 for β-CN 6P; 18,181 for β-LG; 14,180 for α-LA and 66,318 for serum albumin.
    Idioma originalEnglish
    Pàgines (de-a)11-19
    RevistaJournal of Dairy Science
    Volum83
    Número1
    DOIs
    Estat de la publicacióPublicada - 1 de gen. 2000

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