Binding of commercial diuretics with bovine serum albumin.

• GOTO SHIGERU

• ODAWARA YOKIKO

• NAKANO MISAO

• ARAKI YASUNORI

Abstract

The binding of seven commercial diuretics with bovine serum albumin (BSA) was investigated at three different temperatures, 5°, 30° and 37°, by the equilibrium dialysis method and at 37° by the dynamic dialysis method. The binding data of diuretics were described on the basis that the sites per BSA molecule can be divided into two classes, except that of hydrochlorothiazide, and each class characterized by the binding constants, K₁, n₁, and K₂, n₂. The thermodynamic values, ⊿G°, ⊿H°, and ⊿S°for the primary site of binding were determined, and were discussed on the basis of the fact that a hydrophobic interaction is formed between diuretics and BSA. It was also shown that there are sizable negative entropy and enthalpy changes in the binding of ethacrynic acid and BSA, and that hydrochlorothiazide is bound very weakly with BSA and has a remarkable diffusion pattern through cellulose membrane in the dynamic dialysis.

Journal

• Chemical and Pharmaceutical Bulletin

  Chemical and Pharmaceutical Bulletin 26 (8), 2298-2304, 1978

  The Pharmaceutical Society of Japan

Keywords

• hydrophobic interaction

Details

• CRID: 1390282679146748416
• NII Article ID: 110003623293
• NII Book ID: AA00602100
• DOI: 10.1248/cpb.26.2298
• COI: 1:CAS:528:DyaE1cXlvFSqs74%3D
• ISSN: 13475223
• ISSN: 00092363
• PubMed: 709692
• Web Site: http://www.jstage.jst.go.jp/article/cpb1958/26/8/26_8_2298/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/1979093735
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
• Abstract License Flag: Disallowed