Abstract
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.
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© 1978 Springer-Verlag Berlin Heidelberg
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Fehske, K.J., Wollert, U. (1978). Drug Binding Properties of Tyrosine-Modified Human Serum Albumin. In: Deutsche Pharmakologische Gesellschaft. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-39532-5_13
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DOI: https://doi.org/10.1007/978-3-662-39532-5_13
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-38666-8
Online ISBN: 978-3-662-39532-5
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