Premium
NON‐ENZYMIC INCORPORATION OF AMINES INTO PROTEOLIPID PROTEIN 1
Author(s) -
Mokrasch L. C.,
Andelman R.
Publication year - 1968
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1968.tb06839.x
Subject(s) - tryptamine , chemistry , amine gas treating , ovalbumin , proteolipid protein 1 , biochemistry , casein , myelin proteolipid protein , histamine , proteolysis , stereochemistry , organic chemistry , enzyme , biology , immune system , immunology , endocrinology , myelin basic protein , myelin , neuroscience , central nervous system
—Proteolipid protein binds biogenic amines irreversibly. The bound amines can be recovered as the original compounds and as complexes with polypeptide after proteolysis or acid hydrolysis. The properties of the protein‐bound tryptamine are consistent with the concept that the amine is covalently linked by its primary amine group. Mescaline, 3,4‐dihydroxyphenylethylamine, 5‐hydroxytryptamine (5‐HT) and histamine also bind irreversibly to proteolipid protein. 5‐Hydroxytryptamine and mescaline bind similarly to other proteins (casein, ovalbumin, serum albumin and a serum protein mixture), but proteolipid binds the amines to a greater extent.