6533b85efe1ef96bd12bfaa3

RESEARCH PRODUCT

Drug Binding Properties of Tyrosine-Modified Human Serum Albumin

K. J. FehskeU. Wollert

subject

biologyChemistryAlbuminSerum albuminPlasma protein bindingHuman serum albuminBiochemistrybiology.proteinmedicineBinding siteTyrosineBovine serum albuminProtein secondary structuremedicine.drug

description

Human serum albumin (HSA) has only a small number of specific binding sites for drugs. There are facts indicating that tyrosine residues may be involved in these binding sites. Thus we modified HSA with tetranitromethan, a reagent specific for tyrosine residues in proteins. As derived from an UV-absorption quotient three albumins with a degree of modification of two, five and eight residues per molecule were obtained. Only for the albumin with eight residues modified a small reduction of ordered secondary structure was found.

yearjournalcountryeditionlanguage
1978-01-01
https://doi.org/10.1007/978-3-662-39532-5_13