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Hypothalamic cathepsin D: Assay and isoenzyme composition
Author(s) -
Akopyan T. N.,
Barchudaryan N. A.,
Karabashyan L. V.,
Arutunyan A. A.,
Lajtha A.,
Galoyan A. A.
Publication year - 1979
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490040505
Subject(s) - chemistry , endopeptidase , biochemistry , chromatography , cathepsin d , isoelectric focusing , cathepsin , sephadex , microbiology and biotechnology , enzyme , biology
A sensitive and convenient method of endopeptidase assay using as substrate globin modified with pyridoxal‐5‐phosphate was used for determination of acid proteinases in bovine hypothalamus separated by isoelectric focusing. The soluble protein fraction of hypothalamus upon elution from Sephadex gave five peaks of proteinase activity at pH 3.2. The properties indicate that these peaks of endopeptidase activity are isoenzyme forms of cathepsin D.