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Multiple forms of serum aminopeptidases separated by micro two‐dimensional electrophoresis under non‐denaturing conditions
Author(s) -
Sanderink GerJan C. M.,
Artur Yves,
Galteau MarieMadeleine,
WellmanBednawska Maria,
Siest Gérard
Publication year - 1986
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150071008
Subject(s) - aminopeptidase , enzyme , chemistry , biochemistry , papain , electrophoresis , alanine , antiserum , leucine , biology , chromatography , microbiology and biotechnology , amino acid , antibody , immunology
Micro two‐dimensional electrophoresis in the absence of denaturing agents allowed the analysis of the multiple forms of serum aminopeptidases, including their multimolecular complexes, and the detection of their enzymatic activity towards different substrates. Two forms of alanine aminopeptidase (E.C. 3.4.11.2.), differing in sialic acid content, were detected in sera of healthy subjects. In sera of patients with hepatobiliary diseases a large number of additional spots was observed, some of them identified as multimolecular complexes, probably formed by an amphiphilic form of alanine aminopeptidase. Papain treatment resulted in the dissociation of the complexes and in the appearance of a light form of the enzyme in normal sera, which was otherwise only present in pathological samples. Additional spots corresponding to cysteine aminopeptidase (E.C. 3.4.11.3.) were detected in pregnancy sera.