Identification of mouse crystallins in 2D protein patterns by sequencing and mass spectrometry. Application to cataract mutants.
The eye lens proteins of the mouse were separated into 1940 polypeptide spots by two-dimensional electrophoresis in large gels. All 16 crystallins ubiquitous in mammals were identified by protein sequencing and mass spectrometry except for (gamma)-F, which shows an almost identical sequence with (gamma)-E. Two crystallins, (beta)-A2 and (gamma)-S, were shown for the first time to occur in the mouse lens. An investigation of the murine cataract mutant Cat2(nop)((gamma)-B gene) demonstrated that a monogenic mutation might affect a broad spectrum of proteins.
Max-Planck-Institut für Infektionsbiologie, Proteinanalytik, Berlin, Germany.
P R
PR
Jungblut
A
A
Otto
J
J
Favor
M
M
Löwe
E C
EC
Müller
M
M
Kastner
K
K
Sperling
J
J
Klose
D000595:Amino Acid Sequence; D000818:Animals; D002386:Cataract / Q000235:genetics / Q000378:metabolism*; D003459:Crystallins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D013058:Mass Spectrometry; D051379:Mice; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry / Q000235:genetics; D017421:Sequence Analysis
D003459:Crystallins; D010455:Peptides