Characterization of a 43 kD protein associated to aminopeptidase A from murine kidney

Biol Chem Hoppe Seyler. 1994 Sep;375(9):623-7. doi: 10.1515/bchm3.1994.375.9.623.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry*
  • Actins / isolation & purification
  • Amino Acid Sequence
  • Aminopeptidases / chemistry*
  • Aminopeptidases / isolation & purification
  • Animals
  • Blotting, Western
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Glutamyl Aminopeptidase
  • Kidney Tubules, Proximal / enzymology*
  • Mice
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / chemistry
  • Peptide Fragments / isolation & purification
  • Protein Binding
  • Sequence Homology, Amino Acid
  • Trypsin

Substances

  • Actins
  • Peptide Fragments
  • Aminopeptidases
  • Glutamyl Aminopeptidase
  • Trypsin