Premium
ELECTROPHORETIC STUDY OF 5‐HYDROXYTRYPTOPHAN DECARBOXYLASE FROM BRAIN AND LIVER IN SEVERAL SPECIES
Author(s) -
CavalliSforza L. L.,
Santachiara S. A.,
Wang L.,
Erdelyi E.,
Barchas J.
Publication year - 1974
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.1471-4159.1974.tb04385.x
Subject(s) - electrophoresis , acrylamide , biochemistry , carboxy lyases , urea , enzyme , chemistry , 5 hydroxytryptophan , microbiology and biotechnology , biology , polymer , serotonin , organic chemistry , copolymer , receptor
—An electrophoretic investigation in acrylamide gels of 5‐hydroxytryptophan decarboxylase, obtained mostly from mouse, rat, and beef brain and also from beef and human liver, showed electrophoretic differences between species. With the exception of the rat, only one molecular species was found (the same in beef brain and liver). In the rat, polymers form spontaneously and are, at least in part, disaggregated by urea and by triton. Mouse‐rat or beef‐rat molecular hybrids form in the admixtures. No electrophoretic differences were found in five mice strains that were investigated. Techniques of electrophoretic analysis and of assay of 5‐hydroxytryptophan decarboxylase are described, which can be easily applied to other enzymes, provided a substrate is available in radioactive form.