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At least 685 records · Page 38Linked to original sources
PubMed1984

Interaction of synthetic signal sequence fragments with model membranes.

Peptide fragments corresponding to the signal sequence of chicken lysozyme, labelled with the fluorescent 5-dimethylaminonaphthalene-1-sulfonyl (dansyl) group have been synthesized. The emission characteristics and fluorescence polarization of the dansyl group have been used to study the interaction of signal sequence fragments with liposomes. The peptide fragments bind to liposomes and are associated with the hydrophobic core of the bilayer.

Dansyl Compounds↗
PubMed1984

Fluorescence changes from single striated muscle fibres injected with labelled troponin C (TnCDANZ).

A fluorescently labelled derivative of the calcium binding subunit of troponin, TnC, has been injected into isolated striated muscle fibres from the barnacle Balanus nubilus. The Ca2+ affinity of isolated TnC is close to that of intact troponin when located in the thin filament. Excitation of the TnCDANZ within the muscle cell (325nm) revealed a marked fluorescence at 510 nm and was similar to that observed in vitro, which was absent at 400 or 600 nm after subtraction of the fibre autofluorescence. High Ca2+ salines increased the fluorescence at 510 nm by roughly 2 times. Single voltage clamp pulses produced a rapid rise in fluorescence at 510 nm after allowing for any non-specific changes at 400 nm, and this signal preceded force development by approx. 55 ms at 22 degrees C. It reached a maximum at the same time as force and subsequently decayed more slowly. The fluorescence signal increased in magnitude with increase in stimulus intensity. These results suggest that Ca2+ attaches rapidly to the contractile filament, but is lost relatively slowly and imply a slow decay of the activation process.

Animals↗
PubMed1986

Interaction of actin with dansyl-tropomyosin.

5-[Dimethylamino]naphthalene-1-sulfonyl chloride (dansyl chloride) reacts with rabbit skeletal muscle tropomyosin (TM) to yield a highly fluorescent product, DNS-TM. The extent of modification of TM can be regulated over a wide range, 0.3-15.5 dansyl groups per TM, depending upon the temperature and duration of the reaction. However, under all conditions employed, about 15 different fluorescent tryptic peptides of TM were produced. DNS-TM undergoes end-to-end polymerization at low ionic strengths, but to a somewhat lesser extent than unlabelled TM does. DNS-TM also binds muscle F-actin. This interaction may be followed fluorimetrically by observing a blue-shift in emission maximum, an increase in fluorescence intensity or an increase in fluorescence polarization of the DNS-TM complex with F-actin.

Actins↗
PubMed1986

A new sensitive Edman-type reagent: 4-(N-1-dimethylaminonaphthalene-5-sulfonylamino)phenyl isothiocyanate. Its synthesis and application for micro-sequencing of polypeptides.

A new fluorescent PITC homologue Edman-type reagent, 4-(N-1-dimethylaminonaphthalene-5-sulfonylamino)phenyl isothiocyanate (DNSAPITC), was synthesized following a simple three-step synthetic route. The reagent was crystallized and characterized by thin-layer chromatography, IR and electron impact mass spectrometry. Reference DNSAPTH-amino acid derivatives were prepared and a two-dimensional chromatography system on micro-polyamide sheets was developed for separating this mixture. On these sheets the sensitivity was 1-5 pmol, by exposure at 366 nm. Model peptides and proteins were subjected to Edman degradations with this new reagent. A similar coupling efficiency and repetitive degradation yield to those of PITC were found with this reagent. The advantages and limitations of this reagent for sensitive microsequencing are discussed.

Amino Acid Sequence↗
PubMed1987

Identification of the active site of Citrobacter freundii beta-lactamase using dansyl-penicillin.

The active site sequence of a beta-lactamase encoded by chromosomal gene(s) in Citrobacter freundii GN346 was determined using dansyl-penicillin as a fluorescent probe. The tryptic digest of the labelled enzyme gave a fluorescent peptide containing 22 amino acids. The sequence of this peptide was identical to the consensus sequence of class C beta-lactamases, Gly-Ser-X-Ser-Lys. The residue labelled was the serine adjacent to the glycine. The active site sequence corresponded to positions 46-67 of the entire sequence of the Citrobacter freundii beta-lactamase determined on the basis of the DNA sequence of the structural gene [(1986) Eur. J. Biochem. 156, 441-445]. The labelled serine corresponded to Ser-64.

Amino Acid Sequence↗
PubMed1991

Identification and primary structure of a calbindin 9K binding domain in the plasma membrane Ca2+ pump.

Bovine calbindin 9K has been conjugated to a bifunctional, photoactivatable, cleavable and radioactive cross-linker. It has been photolyzed in the presence of preparations of the purified erythrocyte Ca2+ pump, and shown to interact with it in the presence of Ca2+. The affinity of the interaction has been studied using the fluorescence enhancement of dansylated calbindin 9K incubated with the synthetic calmodulin binding domain of the pump. Two versions of the domain have been used, one corresponding to its full length (28 residues), one to about 2/3 of it (20 residues). The affinity of the interaction was between 5 and 10 times lower than in the case of calmodulin.

Amino Acid Sequence↗
PubMed1991

Cellular incorporation and localization of fluorescent derivatives of gangliosides, cerebroside and sphingomyelin.

Fluorescent dansyl derivatives of 3 natural sphingolipids (gangliosides, cerebroside and sphingomyelin) were shown to be readily taken up by culture cells (HeLa-, MDCK- and primary rat brain cells). A part of the incorporated fluorescent sphingolipids remained associated with the cells after incubation in a culture medium containing serum, showing a cellular integration of these lipids. Microscopical studies indicated a localization of incorporated lipids in distinct subcellular regions; whereas dansyl cerebroside densely stained structures suggestive of the cytoskeleton and the actin filament, dansyl sphingomyelin and dansyl gangliosides were primarily associated with the plasma membrane. The findings are consistent with the current views on the arrangement of sphingolipids in animal cells.

Animals↗
PubMed1992

Carbohydrate binding specificity of the Tn-antigen binding lectin from Vicia villosa seeds (VVLB4).

2-Dansylamino-2-deoxy-D-galactose (GalNDns) is a useful fluorescent probe to study the interaction of non-fluorescent sugars with the B4 lectin from Vicia villosa seeds (VVLB4). Binding of the lectin to GalNDns leads to a 5.2-fold increase in Dansyl fluorescence with a concomitant 10 nm blue shift in its emission maximum. The strong binding of GalNDns (Ka = 7.33 x 10(4) M-1 at 20 degrees C) is due to a favourable entropic contribution to the association process. Among the other sugars studied, GalNAc alpha 1-O-Ser followed by Me alpha GalNAc are the best ligands. 2-Deoxygalactose, galactosamine and galactose are 2013, 469 and 130 times weaker ligands, respectively, as compared to GalNAc, whereas GalNDns is about 2.44 times more potent than GalNAc, indicating that substitutions at the C-2 position of GalNAc have a considerable influence on the binding affinities. Equatorial orientation of the hydroxyl group at C-3 and axial orientation at C-4 as in galactose are important for the interaction with VVLB4. The C-6 hydroxyl group is not indispensable. The binding site of the lectin is directed exclusively towards monosaccharides alone. Interestingly enough, despite its preference for Me alpha GalNAc over Me beta GalNAc, in oligosaccharides, the lectin prefers terminal beta-linked GalNAc as compared to the alpha-linked one.

Antigens↗
PubMed1992

The binding of the fluorescent ATP analogue 2'(3')-trinitrophenyladenosine-5'-triphosphate to rat liver fatty acid-binding protein.

The less polar fluorescent analogue of ATP, 2'(3')-trinitrophenyl-5'-triphosphate bound to rat liver fatty acid-binding protein with high affinity (Kd 6.3 x 10(-6) M) and 1:1 molar stoichiometry. This probe bound to the fatty acid binding site of the protein and was displaced by oleic acid and oleoyl CoA. High concentrations of ATP did not cause significant displacement of the fluorescent ATP analogue. Since the anionic part of this molecule is the triphosphate group it is difficult to envisage this group being accommodated at an anion binding site within the non-polar core of this protein as is the case with other fatty acid binding proteins. Therefore it is anticipated that the ligand must bind to liver fatty acid-binding protein with this triphosphate group surface exposed. Caution must be exercised when using the more hydrophobic fluorescent analogue of ATP to investigate the ATP binding properties of proteins.

Adenosine Triphosphate↗