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....

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Bibliographic Details
Published inBiological chemistry Hoppe-Seyler Vol. 375; no. 9; p. 623
Main Authors Mentzel, S, de Leeuw, E P, van Son, J P, Dijkman, H B, de Jong, A S, Koene, R A, Assmann, K J
Format Journal Article
LanguageEnglish
Published Germany 01.09.1994
Subjects
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
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Summary: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.
ISSN:0177-3593
DOI:10.1515/bchm3.1994.375.9.623