The kinetics of dissociation of chlorine pentafluoride

Blauer, Jay A.; McMath, Henry G.; Jaye, F. C.; Engleman, V.S.

doi:10.1021/j100701a005

Cited by 9 publications

(10 citation statements)

References 2 publications

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“…Bilirubin, upon forming a complex with albumin, exhibits strong ellipticities in the visible region of the spectrum (28). This reflects an asymmetric structure of the bilirubin molecule imposed upon it by the conformation of the protein at the high-affinity binding site.…”

Section: Resultsmentioning

confidence: 99%

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Gitzelmann-Cumarasamy

Gitzelmann²,

Wilson

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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The existence of a functionally immature fetal albumin has been postulated to explain the reduced ability of newborn plasma to bind bilirubin and various drugs. In support of this, cord and adult albumin, isolated by a simple salting-out technique, were reported to differ in electrophoretic and chromatographic properties and in their resistance to alkali and proteolytic enzymes. However, the interpretation of these findings has since been questioned. To resolve this controversy, we have purified to homogeneity human serum albumins from pooled umbilical cord and adult donor plasma. The two albumins were compared and found to be indistinguishable by polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate, as well as by immunoelectrophoresis and double immunodiffusion using specific antibodies against both albumins. Furthermore, the amino acid compositions, the aminoterminal sequence (Asp-Ala-His-Lys-Ser-Glu-Val-Ala-), the carboxy terminus (Leu), and the peptide fingerprints were identical in the two albumins. No significant differences were found by circular dichroism in the ultraviolet (200-350 nm). Binding studies with bilirubin showed association constants of 3.7 + 0.7 X 107 M-1 for cord and 2.9 : 0.3 X 107 M-' for adult albumin, respectively. The circular dichroic spectra of 1:1 bilirubin-albumin complexes showed considerable variation between the batches but were not significantly different. The only difference was found in the fluorescence spectra of the bilirubin-albumin complexes, in which complexes with adult albumin showed only 75% of the relative fluorescence exhibited with cord albumin. The combined results nevertheless strongly indicate that fetal and adult albumins are very similar, if not identical. Human serum albumin is an almost universal carrier for a host of metabolites and drugs (1). As such it plays a central role in the regulation of their activity or toxicity. This is of particular significance in neonatal medicine because newborns, with their immature detoxifying mechanisms (for review see ref.2), are highly susceptible to various toxic agents. A well-known example is bilirubin encephalopathy resulting from neonatal jaundice.During clinical studies it was observed that newborn serum has a lower ability to bind bilirubin and drugs than adult serum does (refs. 3 and 4 and references cited therein). To explain these observations, the existence of a fetal type of albumin, analogous to hemoglobin F, was postulated. In support of this, cord and adult albumin, isolated by a simple salting-out technique, were reported to differ in electrophoretic and chromatographic properties and to vary in resistance to alkali and proteolytic enzymes (5, 6). However, authors of subsequent papers questioned the existence of a functionally immature albumin and attributed the reduced binding of newborn serum to competitive binding by increased concentrations of certain metabolites such as arachidonic acid and hematin (7-11).To resolve this controversy, we purified cord and adult albumin...

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Section: Resultsmentioning

confidence: 99%

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Gitzelmann-Cumarasamy

Gitzelmann²,

Wilson

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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“…The applicability of albumin in BR removal is limited by the large amount of bound BSA required to remove significant amounts of bilirubin. Its high BR specificity and the fact that albumin immobilization onto natural or synthetic polymeric supports improves their biocompatibility [26], however, led to an extensive use of BSA as bioligand in studies of BR removal [27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Adsorptive membranes for bilirubin removal

Avramescu

Sager

Borneman

et al. 2004

Journal of Chromatography B

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“…[BR] i and [BSA] i are both at 2 ϫ 10 -5 mol dm -3 and K b equals 5·7 ϫ 10 6 dm 3 mol -1 [58]. On solving the above quadratic equation one arrives at a value for f c = 0·91 or 1·09 and it can therefore be concluded that a minimum of 91% BR is bound to BSA.…”

Section: ·2mentioning

confidence: 97%