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At least 415 records · Page 23Linked to original sources

PubMed1987

Fluorescence and phosphorescence of adrenolutin.

Adrenolutin 3,5,6-trihydroxy-1-methylindole is an intermediate in the metabolism of adrenaline and in the formation of adrenochromo-melanins. Excitation and emission spectra, quantum yield of the adrenolutin fluorescence in water, D2O, ethanol, methanol, acetone and aqueous phosphate buffer at different pH at 293K temperature are reported. Dependence of the quantum yield of adrenolutin on its concentration are measured. Lifetimes of 0.1 mM adrenolutin in water and ethanol are 32.0 +/- 0.2 ns and 9.2 +/- 0.2 ns respectively. Also fluorescence and phosphorescence spectra of adrenolutin in methanol at 110K are obtained. Degrees of polarization and angles between the dipoles for the three main bands absorption of adrenolutin from measurements at 103K are calculated. Adrenolutin may be classified as one of the most strongly fluorescing metabolites. Broad excitation spectrum and high quantum yields make this compound a potential effective acceptor of excitation energy.

Indoles↗

PubMedDate not supplied

[Study of conformation transitions in proteins by tryptophan fluorescence and phosphorescence at low temperatures].

The well-known conformational changes in proteins containing a single tryptophan residue, such as pH-induced N-->F transition in human serum albumin, pH-induced acidic transition in cod parvalbumin, and KCl-induced tetramerization of bee venom melittin were monitored by changes in low temperature phosphorescence and fluorescence spectra suggesting two independent series of normal components. Parameters of low temperature tryptophan luminescence were sensitive to chromophore environment. A correlation of changes of some spectral parameters with accessibility of tryptophan to water was revealed, however, spectral changes mainly depend on specific interactions of the chromophore with its environment.

Animals↗

PubMed1994

[Study of the rotational mobility of E1- and E2- conformers of Ca-ATPase in sarcoplasmic reticulum membranes using a time-resolved phosphorescence anisotropy method].

Membrane preparations of sarcoplasmic reticulum Ca-ATPase from rabbit skeletal muscles were covalently labelled with eosin-5'-isothiocyanate at Lys 515 residue in a putative active site and with 4-(iodoacetamido)-eosin (presumably, at Cys 670 and Cys 674 residues). These preparations were used to measure the laser flash induced phosphorescence anisotropy in a microsecond time scale. An analysis of effects of diethyl ether, glycerol, the nonionic detergent C12E9 and Ca-ATPase ligands stabilizing the enzyme in the E2 or E1 conformeric state, on the anisotropy parameters showed that Ca-ATPase of sarcoplasmic reticulum membranes is present in both monomeric and oligomeric states. The enzyme transition from the E1 to the E2 conformation is due to the increase in the content of oligomeric complexes and their average size. These data support the hypothesis that the oligomeric state of Ca-ATPase can be changed during enzyme reaction cycle.

Animals↗

PubMed1950