Abstract
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 αs1-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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
