Multidimensional fractionation of the bovine skeletal muscle proteome.
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.
Cruzado-Park
Ingrid D
ID
Beckman Coulter, Fullerton, California, USA. idcruzado@beckman.com
Betgovargez
Edna
E
Ratnayake
Chitra
C
Simonian
Michael H
MH
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
D020543:Proteome; D009113:Muramidase