On the Identity of DOPA Decarboxylase and 5-Hydroxytryptophan Decarboxylase
AUTOR(ES)
Christenson, James G.
RESUMO
Simultaneous immunological titration of DOPA and 5-hydroxytryptophan decarboxylase activities, from a number of tissues of various species, showed that the two activities were not distinguishable with a monospecific antiserum to hog kidney decarboxylase. Together with previous findings, these data firmly establish the concept that in mammalian tissues the two enzyme activities are associated with a single protein, namely aromatic L-amino acid decarboxylase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=426454Documentos Relacionados
- Biopterin synthesis defect. Treatment with L-dopa and 5-hydroxytryptophan compared with therapy with a tetrahydropterin.
- Formation of 5-hydroxykynurenine and 5-hydroxykynurenamine from 5-hydroxytryptophan in rabbit small intestine
- Selective incorporation of 5-hydroxytryptophan into proteins in mammalian cells
- beta-Endorphin: development of tolerance and its reversal by 5-hydroxytryptophan in cats.
- Double-blind clinical trial of 5-hydroxytryptophan in a case of Lesch-Nyhan syndrome.
