Identification of beta protein precursor in newborn rat brain.
We have identified by protein sequencing the precursor of beta protein in newborn rat brain. A rabbit antibody was raised against a synthetic peptide corresponding to the carboxyl-terminal 30 residues (666-695) of the putative beta-amyloid protein precursor (Kang et al. 1987). The antiserum recognized multiple bands at 110-130 kD in the blot of Triton X-100 extract of newborn rat brain homogenates. The partially purified immunoreactive proteins were subjected to SDS-PAGE, electrophoretically transferred onto a polyvinylidene difluoride membrane and analyzed for the partial amino-terminal sequence. Each of the three major immunoreactive polypeptides yielded the same amino-terminal sequence of LEVPTxGNAgxL (x: unidentified, g: weakly assigned glycine) which corresponds to the residues 18-29 of the putative precursor.
Takio
K
K
Frontier Research Program, RIKEN, Saitama, Japan.
Hasegawa
M
M
Titani
K
K
Ihara
Y
Y
D000544:Alzheimer Disease; D000595:Amino Acid Sequence; D000682:Amyloid / Q000032:analysis*; D016564:Amyloid beta-Protein Precursor; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism*; D001923:Brain Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D015151:Immunoblotting; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000032:analysis*; D011498:Protein Precursors / Q000032:analysis*; D051381:Rats
D000682:Amyloid; D016564:Amyloid beta-Protein Precursor; D011480:Protease Inhibitors; D011498:Protein Precursors