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Identification of mouse crystallins in 2D protein patterns by sequencing and mass spectrometry. Application to
P R Jungblut1, A Otto, J Favor
1Max-Planck-Institut für Infektionsbiologie, Proteinanalytik, Berlin, Germany.
FEBS Letters
|October 8, 1998
Abstract:
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.