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Biomedical subjects

A F Agrò

Publications and source records attributed to A F Agrò.

At least 37 records · Page 2Linked to original sources
PubMed1984

Interaction of terbium with human platelets.

The effect of terbium on platelets has been studied by aggregation experiments and by fluorescence measurements. TbCl3 does not substitute for CaCl2 in the aggregation of platelets induced by ADP, but it may even inhibit, probably by a competition mechanism. It was impossible to observe a sensitized emission of Tb3+ in the presence of platelets. Instead the lanthanide, like Ca2+, significantly increases the aggregation of platelets induced by A23187. The fluorescence yield of this compound is greater in the presence of platelets than in buffer alone. Energy transfer appears to take place from the aromatic amino acids of the platelet membrane to the bound ionophore.

Adenosine Triphosphate↗
PubMed1980

Luminescence of carbon monoxide hemocyanins.

The effect of carbon monoxide on the luminescence properties of Helix pomatia alpha-hemocyanin and Panulirus interruptus hemocyanin has been studied. These proteins, when saturated with carbon monoxide, show, besides the intrinsic fluorescence arising from the aromatic amino acid residues, emission in the visible region with a maximum between 540 and 560 nm. Results of carbon monoxide titration experiments and data from absorption and excitation-emission spectra provide convincing evidence that the observed emission originates from a fluorescent copper(I)-carbon monoxide complex, and this emission is interpreted as charge-transfer luminescence.

Animals↗
PubMed1977

On the nature of chromophore in pig kidney diamine oxidase.

The nature of the 500-nm chromophore in pig kidney diamine oxidase was investigated by absorption spectroscopy and fluorescence in the presence of various chelating or carbonyl-specific reagents. From the spectroscopic measurements the following conclusions can be drawn. First, the 500-nm absorption band is not due to copper, the reduction of which is not related to the disappearance of this band. Second, phenylhydrazine and cycloserine give rise, upon reaction with the enzyme, to absorptions very similar to those of a pyridoxal enzyme, aspartate aminotransferase. Third, these enzyme derivatives are unexpectedly non-fluorescent. Copper removal, obtained after prolonged incubation of cycloserine-treated enzyme in the presence of reducing and chelating agents, leads to a fluorescence similar to that of cycloserine-aspartate transminase. It is proposed that copper is coordinated to the postulated pyridoxal phosphate of diamine oxidase through the pyridine nitrogen.

Amine Oxidase (Copper-Containing)↗