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  • Title: In vivo and in vitro binding of fatty acids to genetic variants of human serum albumin.
    Author: Kragh-Hansen U, Nielsen H, Pedersen AO.
    Journal: Int J Clin Pharmacol Res; 1995; 15(2):33-43. PubMed ID: 8593972.
    Abstract:
    The effect of genetic variation on the fatty-acid binding properties of human serum albumin was studied by two methods involving the use of sequenced albumin variants isolated from bisalbuminaemic persons. First, the amount of total fatty acid and of several individuals fatty acids bound to eighteen different variants and to their normal counterpart (Alb A) were determined by a gas-chromatographic micromethod. Pronounced effects on total fatty acid binding were found for the glycosylated variants Alb Redhill (modified in domain II) and Alb Casebrook (domain III) in which cases a 1.7- and 8.6-fold increment, respectively, was found. By contrast, Alb Malm0 (glycosylated in domain I) carried the same amount of fatty acid as Alb A. The fatty acid loads on three chain-termination variants were normal. Finally, eight albumins with single amino-acid substitutions bound normal amounts of fatty acid, whereas one bound increased (1.7-fold) and three albumins bound diminished amounts (0.5-0.6-fold). Information on nineteen individual fatty acids was also obtained. It was possible, based on the type of changes in their relative amounts, to group the fatty acids as follows: (a) = C6:0 - C14:0, (b) = C15:0 - C18:0, (c) = C16:1 - C18:1, and (d) a group composed of essential and conditionally essential fatty acids. For nine variants, in most cases modified in domain III, large changes in one or more of these groups were observed. The changes were not related to any changes in total fatty acid load. Second, the binding of laurate, as a representative of the group (a) fatty acids, to delipidated albumin preparations was studied at pH 7.4 by a kinetic dialysis technique. The first stoichiometric association constant for binding to Alb Redhill (0.7-fold) and Alb Casebrook (0.6-fold) was diminished as compared with binding to their corresponding Alb A, whereas binding to one chain-termination variant and three single amino-acid substitutions were all unaffected by the mutation.
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