Hypoxanthine uptake by isolated brain microvessels.
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to A Fiori.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
The effect of a number of inhibitors of L-aromatic amino acid decarboxylase activity on the absorption spectrum of the enzyme-bound coenzyme has been studied. It has been observed that the compounds tested, even if devoid of the amino function and therefore unable to form the Schiff base with the coenzyme, modify significantly the enzyme spectrum, indicating their binding to the coenzyme active site. Spectral modifications suggest that at least two kinds of binding of inhibitors to L-aromatic amino acid decarboxylase may occur, depending on their structural features. Moreover, from the spectra obtained at different concentrations of the inhibitors their affinity constants have been determined: data indicate that the cathecol ring gives the largest contribution to the binding, while the presence of the carboxyl group, the aminic group and the aliphatic chain are responsible for a decrease in the binding, which could be relevant for the efficiency of the catalysis.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Two immunoassays are described: mixed agglutination on solid phase (MASP) and inhibition of mixed agglutination on solid phase (IMASP). The MASP assay permits detection and measurement of soluble A, B and H high molecular weight glycoproteins in secretor individuals with a sensitivity at least 800 times greater than the usual inhibition technique. Both secretors and non-secretors can be typed by the less sensitive IMASP test which also permits the detection of low molecular weight A, B and H substances.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
A procedure for 3,4-dihydroxyphenylalanine decarboxylase from pig kkdney purification is described in detail. The preparation has no detectable impurity on electrophoresis and on ultracentrifugation and authors. However two significant differences are observed: a different stimulation of activity by added pyridoxal 5'-phosphate and a nearly complete decarboxylation of L-3,4-dihydroxyphenylalanine in absence of added coenzyme. Absorption, fluorescence and circular dichroism properties of the coenzyme-apoenzyme interaction are also described. The results are consistent with the existence of at least four coenzyme-apoenzyme complexes, three of them active.
The gel-chromatographic behavior of A, B and H substances from urine was examined and compared with that of previously described AHB salivary fractions. Urinary fractions 1 and 2 exhibited a molecular size smaller than those of salivary fractions 1 and 2. In the urine of 52 subjects a polymorphism of A, B and H substances, with four main types, was observed which is independent of the salivary one and of the so-called secretor and nonsecretor status.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.