title: Multidimensional fractionation of the bovine skeletal muscle proteome.
abstract: The ultimate goal of proteomics is to understand complex biological systems. The first step toward this end is the discovery of protein differences by profiling a given proteome. One approach to proteome profiling is to fractionate it into intact proteins, with subsequent identification and quantitation. In this work, lysates of bovine skeletal muscle were prepared. Reproducible proteome profiles were generated by an automatic two-dimensional protein fractionation system. Proteins were separated by isoelectric point and then by hydrophobicity. The data collected from both separations were used to generate proteome profiles. A high protein content fraction with pl above 8.5 was digested with trypsin, and its main protein component was identified as lysozyme C by matrix assisted laser desorption/ionization-time of flight mass spectrometry.
authors.affiliation: Beckman Coulter, Fullerton, California, USA. idcruzado@beckman.com
authors.forename: Ingrid D
authors.initials: ID
authors.lastname: Cruzado-Park
authors.forename: Edna
authors.initials: E
authors.lastname: Betgovargez
authors.forename: Chitra
authors.initials: C
authors.lastname: Ratnayake
authors.forename: Michael H
authors.initials: MH
authors.lastname: Simonian
mesh_terms: D000818:Animals; D002417:Cattle; D005591:Chemical Fractionation; D007526:Isoelectric Point; D009113:Muramidase / Q000032:analysis / Q000302:isolation & purification; D018482:Muscle, Skeletal / Q000737:chemistry*; D020543:Proteome; D040901:Proteomics / Q000379:methods*; D015203:Reproducibility of Results; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D020543:Proteome; D009113:Muramidase