Fluorescent Protein Conjugates

Dandliker, Walter B.; Portmann, Adolf

doi:10.1007/978-1-4684-1878-1_6

Cited by 7 publications

(3 citation statements)

References 212 publications

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“…The fact that the shape of the spectra and the positions of the maxima were the same for both complexes indicates that the conformations of the bound chromophores do not appreciably differ. Theoretically, the lower fluorescence quantum yield observed with the adult albumin complex could be due to any of the following three mechanisms (31)(32)(33): (i) absorption of irradiating light by extraneous yellow pigments, thereby preventing the excitation of bilirubin; (ii) absorption of radiation emitted from excited bilirubin by a red pigment; or (iii) conversion of the excitation energy into heat by dissipation through vibrational pathways (34). In our samples, modes i and ii can be excluded because the absorption spectra of the albumin preparations gave no indication of the presence of colored contaminants.…”

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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“…Several studies have appeared recently applying fluorescence resonance energy transfer (FRET) to determine structural features related to distances between fluorophores that are covalently linked to specific positions of DNA (Cardullo et al 1988;Murchie et al 1989;Cooper & Hagerman, 1990;Clegg et al 1992;Rippe et al 1993). Although varying degrees of success have been reported in determining the detailed structural information of nucleic acids using covalently linked fluorophores, it is clear that this method will find many applications in the future, as is already the case, for instance, for protein studies (Dandliker & Portmann, 1971).…”

Section: Fluorescence Resonance Energy Transfermentioning

confidence: 99%

The structure of branched DNA species

Lilley

Clegg

1993

Quart. Rev. Biophys.

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“…The idea of extrinsic labeling was extended by the discovery of Weber & Laurence (l34) that a variety of polycyclic aromatic com pounds that were nonfluorescent in aqueous media became fluorescent upon binding serum albumin. A series of classic papers by Weber and his colleagues led the way in the use of fluorescence spectroscopy as a tool to study the structure and dynamics of proteins and other macro molecules (24,93,107,133). A wide range of reactive fluorescent dyes is now available that can be used to target specific sites, exhibit environ mental sensitivities, and fit into specific spectral regions (45,125).…”

Section: Fluorescent Analogues Of Proteinsmentioning

confidence: 99%

Fluorescent Protein Biosensors: Measurement of Molecular Dynamics in Living Cells

Giuliano

Post

Hahn³

et al. 1995

Annu. Rev. Biophys. Biomol. Struct.

107

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A new generation of reagents that report on specific molecular events in living cells, called fluorescent protein biosensors, has evolved from in vitro fluorescence spectroscopy and fluorescent analogue cytochemistry. Creative designs of fluorescent protein biosensors to measure the molecular dynamics of macromolecules, metabolites, and ions in single cells emerge from the integrative use of contemporary synthetic organic chemistry, biochemistry, and molecular biology. Future advances in fluorescent probe design, computer-driven optical instrumentation, and software will allow us to engineer endogenous cellular components that localize and function as reporters of their activities, thus moving molecular measurement beyond the single cell to living tissues and the whole organism.

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Fluorescent Protein Conjugates

Cited by 7 publications

References 212 publications

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

The structure of branched DNA species

Fluorescent Protein Biosensors: Measurement of Molecular Dynamics in Living Cells

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