Premium
Immunological characterization of peptidyl‐glycine‐α‐amidating monooxygenases
Author(s) -
Sharoyan S.G.,
Nalbandyan R.M.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80911-l
Subject(s) - monooxygenase , antibody , enzyme , chemistry , biochemistry , glycine , cytosol , anterior pituitary , microbiology and biotechnology , biology , hormone , amino acid , immunology , cytochrome p450
Antibodies to the soluble form of the copper‐containing enzyme, peptidyl‐glycine‐α‐amidating monooxygenase isolated from secretory granules of bovine pituitary anterior lobes were found to belong to immunoglobulin G 1 . The antibodies were used to study the subcellular distribution of the enzyme in this tissue, and positive tests were found only for granular and cytosol fractions. The antibodies do not crossreact with other copper‐containing systems of secretory granules, such as neurocuprein and dopamine‐ß‐monooxygenase. It was shown that the antibodies give the crossreaction with the enzyme isolated from secretory granules of bovine pituitary anterior lobes, cardiac atria, pancreas and adrenal medulla, indicating the antigenic identity of the enzyme from secretory granules of different glands.