Interaction between bumetanide and human serum albumin

Masami Tanaka, Seizo Masuda, Keiji Minagawa, Takeshi Mori

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The interaction between Bumetanide (BMD) and human serum albumin (HSA) was investigated by equilibrium dialysis. Since the binding constant of BMD to HSA was independent of ionic strength and decreased with increase of alkyl chain length of fatty acid added, the interaction between BMD and HSA was considered to be due to hydrophobic mechanism. Chemical shifts in 1H-NMR spectra of BMD were independent of the concentration of BMD and addition of HSA. Spin-lattice relaxation time (T1) and spin-spin relaxation time (T2) of respective protons of BMD were independent of the concentration, but depended on the concentration of HSA added. The binding position of BMD to HSA was considered to involve the hydrophobic aromatic moiety of BMD from the ratio of spin-spin relaxation rates (1/T2) of BMD bound to HSA and free BMD.

Original languageEnglish
Title of host publication54th SPSJ Annual Meeting 2005 - Polymer Preprints, Japan
Pages2063
Number of pages1
Volume54
Edition1
Publication statusPublished - 2005
Externally publishedYes
Event54th SPSJ Annual Meeting 2005 - Yokohama, Japan
Duration: May 25 2005May 27 2005

Other

Other54th SPSJ Annual Meeting 2005
CountryJapan
CityYokohama
Period5/25/055/27/05

All Science Journal Classification (ASJC) codes

  • Engineering(all)

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