The effect of sodium salicylate on the binding ofl-tryptophan to serum proteins
Authors:
- 1 November 1969
- journal article
- Published by Oxford University Press (OUP) in Journal of Pharmacy and Pharmacology
- Vol. 21 (11) , 744-750
Abstract
In human serum, l-tryptophan is the only amino-acid bound to protein. Salicylate causes a release of tryptophan from its binding sites on human serum proteins and bovine albumin. Some implications of this finding are discussed.Keywords
This publication has 13 references indexed in Scilit:
- LOCAL ANTIPHLOGISTIC ACTIVITY OF l -PHENYLALANINE AND l -TRYPTOPHANEJournal of Endocrinology, 1968
- Excretion of tryptophan metabolites in rheumatoid arthritisArthritis & Rheumatism, 1966
- Salicylate and aminotransferasesJournal of Pharmacy and Pharmacology, 1965
- Enhancement of Antimicrobial Activity of Penicillins and Other Antibiotics in Human Serum by Competitive Serum Binding Inhibitors.Experimental Biology and Medicine, 1964
- Studies on Purified 3-Hydroxyanthranilic Acid OxidaseJournal of Biological Chemistry, 1962
- Metabolism of Tryptophan in Rheumatoid ArthritisAnnals of the Rheumatic Diseases, 1962
- THE IDENTIFICATION OF A FLUORESCENT REDUCING SUBSTANCE IN THE URINE OF PATIENTS WITH RHEUMATOID ARTHRITISJournal of Clinical Pathology, 1960
- Thyroxine-releasing Effect of Salicylate and of 2,4-DinitrophenolNature, 1959
- The Specific Binding of l-Tryptophan to Serum AlbuminJournal of Biological Chemistry, 1958
- THE CONVERSION OF TRYPTOPHAN TO KYNURENINE IN LIVERJournal of Biological Chemistry, 1950