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A simple model for circadian timing by mammals BJMBR
Cardoso,F.R.G.; de O. Cruz,F.A.; Silva,D.; Cortez,C.M..
Circadian timing is structured in such a way as to receive information from the external and internal environments, and its function is the timing organization of the physiological and behavioral processes in a circadian pattern. In mammals, the circadian timing system consists of a group of structures, which includes the suprachiasmatic nucleus (SCN), the intergeniculate leaflet and the pineal gland. Neuron groups working as a biological pacemaker are found in the SCN, forming a biological master clock. We present here a simple model for the circadian timing system of mammals, which is able to reproduce two fundamental characteristics of biological rhythms: the endogenous generation of pulses and synchronization with the light-dark cycle. In this model,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Circadian cycle; Coupling oscillators; Kuramoto's model.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2009000100017
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Quenching of the intrinsic fluorescence of bovine serum albumin by chlorpromazine and hemin BJMBR
Silva,D.; Cortez,C.M.; Louro,S.R.W..
The binding of chlorpromazine (CPZ) and hemin to bovine serum albumin was studied by the fluorescence quenching technique. CPZ is a widely used anti-psychotic drug that interacts with blood components, influences bioavailability, and affects function of several biomolecules. Hemin is an important ferric residue of hemoglobin that binds within the hydrophobic region of albumin with high specificity. Quenching of the intrinsic fluorescence of bovine serum albumin (BSA) was observed by selectively exciting tryptophan residues at 290 nm. Emission spectra were recorded in the range from 300 to 450 nm for each quencher addition. Stern-Volmer graphs were plotted, and the quenching constant estimated for BSA solution titrated with hemin at 25ºC was 1.44 (± 0.05) x...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Chlorpromazine; Hemin; Albumin; Fluorescence quenching.
Ano: 2004 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2004000700004
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