Application of electrospray ionization mass spectrometry with maximum-entropy analysis to allelic 'fingerprinting' of major urinary proteins.
Mixtures of a specific group of proteins, the major urinary proteins (MUPs), believed to have a role in odorant binding, have been analysed by electrospray ionization mass spectrometry. The data obtained from conventional transformed electrospray data confirm that the molecular weights of the protein mixtures, deduced from published sequences, lie in the molecular weight range 18,600 to 19,000 Da. Application of maximum-entropy analysis to the raw electrospray data has confirmed a heterogeneity in MUP composition, consistent with allelic similarities (and differences) between the different mouse strains. This work demonstrates the use of maximum entropy in the assessment of protein content and in the subsequent resolution enhancement of naturally occurring protein mixtures containing components of closely similar molecular mass.
Evershed
R P
RP
Department of Biochemistry, University of Liverpool, UK.
Robertson
D H
DH
Beynon
R J
RJ
Green
B N
BN
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D008297:Male; D013058:Mass Spectrometry / Q000379:methods; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D008808:Mice, Inbred CBA; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics*; D011507:Proteinuria / Q000235:genetics* / Q000652:urine
D011506:Proteins; C035737:major urinary proteins