Binding study of the fluorescence probe 1-anilino-8-naphthalensulfonate to human plasma and human and bovine serum albumin using potentiometric titration.

Abstract:

:The binding of 1-anilino-8-naphthalenesulfonate (ANS) to bovine serum albumin (BSA), human serum albumin (HSA), and human plasma has been studied by potentiometric titration utilizing a laboratory constructed ion selective electrode (ISE) of ANS. Three classes of ANS binding sites were found on BSA, HSA, and plasma at 25 and 37 degrees C. Computer analysis of the data resulted in estimates for the association constants, number of binding sites (HSA, BSA), and binding capacity of each class. The association constants for the first class of binding sites at 25 degrees C were found to be 7.53 (+/- 0.59) x 10(5), 2.70 (+/- 0.20) x 10(5), and 2.64 (+/- 0.26) x 10(5) M-1 for BSA, HSA, and plasma, respectively. Lower values for the association constants of all binding classes were estimated at the higher temperature (37 degrees C). The binding capacity for ANS decreased in the order BSA, plasma, HSA.

journal_name

Pharm Res

journal_title

Pharmaceutical research

authors

Valsami GN,Macheras PE,Koupparis MA

doi

10.1023/a:1015855613083

subject

Has Abstract

pub_date

1991-07-01 00:00:00

pages

888-92

issue

7

eissn

0724-8741

issn

1573-904X

journal_volume

8

pub_type

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