Characterization of a 43 kD protein associated to aminopeptidase A from murine kidney.
SDS-PAGE of affinity-purified APA under reducing conditions showed in addition to the specific APA band of M(r) 130 kD, a second band of M(r) 43 kD. Internal amino acid sequencing of three tryptic peptides from this second band, that was cut out of the polyacrylamide gel, matched the actin sequence. The identity of the 43 kD band was also confirmed by Western blotting.
Department of Pathology, University Hospital Nijmegen, The Netherlands.
S
S
Mentzel
E P
EP
de Leeuw
J P
JP
van Son
H B
HB
Dijkman
A S
AS
de Jong
R A
RA
Koene
K J
KJ
Assmann
D000199:Actins / Q000737:chemistry* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000737:chemistry* / Q000302:isolation & purification; D000818:Animals; D015153:Blotting, Western; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D043384:Glutamyl Aminopeptidase; D007687:Kidney Tubules, Proximal / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D014357:Trypsin
D000199:Actins; D010446:Peptide Fragments; D000626:Aminopeptidases; D043384:Glutamyl Aminopeptidase; D014357:Trypsin