1985
DOI: 10.1016/0006-2952(85)90523-4
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Measurement of the association of cholephylic organic anions with different binding proteins

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Cited by 23 publications
(21 citation statements)
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“…In this method, unbound and HSA-bound BSP were separated by the use of Blue Sepharose. The Kd values (between 1.4 and 1.9 µM) obtained with the Blue Sepharose method were very similar to the values reported in the literature, [23][24][25] indicating the validity of this method.…”
Section: Discussionsupporting
confidence: 76%
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“…In this method, unbound and HSA-bound BSP were separated by the use of Blue Sepharose. The Kd values (between 1.4 and 1.9 µM) obtained with the Blue Sepharose method were very similar to the values reported in the literature, [23][24][25] indicating the validity of this method.…”
Section: Discussionsupporting
confidence: 76%
“…[23][24][25] In the present study, we described a new technique for the determination of unbound BSP concentration in the presence of HSA. In this method, unbound and HSA-bound BSP were separated by the use of Blue Sepharose.…”
Section: Discussionmentioning
confidence: 99%
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“…The protein in the presence of DCA binds up to 15 tool BSP/mol protein with a KD of 5 ~tmol/1 (Tiribelli et al 1976). Native bilitranslocase in the absence of DCA showed a lower KD of 1.2 gM and bound BSP at a ratio of 3 mol per mole of protein (Gentile et al 1985b). The protein has been reconstituted into artificial liposomes and in erythrocyte membranes ), both of which transported BSP.…”
Section: Carrier Proteins For Hepatic Uptake Of Cholephilic Organic Amentioning
confidence: 99%
“…It is reversibly bound to a number of proteins, including albumin and lipoprotein [4]. With a dissociation constant (Kd) of 3 pmol It', as found for in uitro binding to bovine albumin [5], more than 99% of ICG will be protein bound in a plasma sample with 1 pmol 1-I of ICG and the physiological albumin concentration of 400-660 pmol I-'.…”
Section: Introductionmentioning
confidence: 97%