1981
DOI: 10.1021/bi00524a033
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Albumin-lipid interactions: prostaglandin stability as a probe for characterizing binding sites on vertebrate albumins

Abstract: We determined the effect of vertebrate albumins on the stability of several physiologically relevant prostaglandins. All naturally occurring prostaglandins with beta-hydroxy ketone group decomposed by first-order kinetics, dependent on the albumin concentration in 0.1 M, pH 7.4, buffer at 37 degrees C. Even subphysiological levels of albumin (1-20 mg/mL) significantly reduced the stability of these compounds in vitro. The prostaglandins with a beta-hydroxy ketone responded to albumin in the order of their intr… Show more

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Cited by 68 publications
(45 citation statements)
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“…The structure changes induced by PGEr appeared to be reversible: after separation of PGEr from the lipoproteins the fluorescence pol~i~tion returned almost to the initial level and after addition of a new portion of PGEr the P value increased again ( fig.3). The effect of PGEr on the fluorescence parameters of ASM-labeled HDL could be reversed also by addition of human serum albumin which effectively binds prostaglandins [8]. Interestingly, removal of PGEi from the HDL surface by addition of albumin resulted in a relatively fast decrease of E and a much slower relaxation of P (fig.4).…”
Section: Resultsmentioning
confidence: 97%
“…The structure changes induced by PGEr appeared to be reversible: after separation of PGEr from the lipoproteins the fluorescence pol~i~tion returned almost to the initial level and after addition of a new portion of PGEr the P value increased again ( fig.3). The effect of PGEr on the fluorescence parameters of ASM-labeled HDL could be reversed also by addition of human serum albumin which effectively binds prostaglandins [8]. Interestingly, removal of PGEi from the HDL surface by addition of albumin resulted in a relatively fast decrease of E and a much slower relaxation of P (fig.4).…”
Section: Resultsmentioning
confidence: 97%
“…These results indicate that this method showed excellent accuracy and precision. PGD 2 is inherently less stable in physiologic solutions than PGE 2 [30]. The instability of PGD 2 was reported in 1983 by Fitzpatrick et al [31,32] who determined that albumin catalyzes the dehydration of PGD 2 in vitro to three products.…”
Section: Methods Validationmentioning
confidence: 99%
“…15,17,[44][45][46] However, the active concentration of free PGs will be considerably lower, since PGs readily bind to serum albumin. [47][48][49][50] Using our conditions, 80% of PGD 2 added to the culture media was bound to serum albumin within 1 h after drug addition. Furthermore, due to the presence of albumin, PGD 2 is readily metabolized to different PGD 2 derivatives.…”
Section: Inhibition Of Pgd 2 Effect By Cycloheximidementioning
confidence: 99%