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Biomedical subjects

E Fioretti

Publications and source records attributed to E Fioretti.

48 records · Page 3Linked to original sources
PubMed1983

Heterogeneity of the basic pancreatic inhibitor (Kunitz) in various bovine organs.

Four protein protease inhibitors (I, II, III, IV) having low molecular weights (10 600-6500) and basic isoelectric points were isolated by affinity chromatography from bovine spleen. Inhibitor IV was identified as the basic pancreatic trypsin inhibitor (Kunitz inhibitor); the presence and distribution of components I, II and III vary in the different bovine organs. Spleen inhibitors I, II, III and IV were purified by ion-exchange chromatography; they form 1:1 complexes with trypsin and inhibit enzymatic activity of trypsin, chymotrypsin and kallikrein. Inhibitors I, II and III contain carbohydrate moieties (7-4%) covalently bound to the polypeptide chain. Specific basic pancreatic trypsin inhibitor antiserum has shown the complete identity between inhibitor IV and the basic pancreatic trypsin inhibitor, while partial cross-reactivity between the basic pancreatic trypsin inhibitor and inhibitors I, II and III can be seen from a double immunodiffusion test.

Animals↗
PubMed1978

Properties of trout hemoglobins reconstituted with unnatural hemes.

Native globins isolated from trout hemoglobin compoents I and IV have been reconstituted with proto-, meso-, and deuteroheme, and the spectral and functional properties of the reconstituted hemoglobins have been investigated. Equilibrium and kinetic studies allow the following conclusions. (a) The properties of the proto-reconstituted hemoglobins are very similar, or indistinguishable, from those of the native Hb's I and IV. (B) The CO binding kinetics for both proteins were found to be consistent with the equilibrium data: the overall association rate constant increases (and the autocatalytic character of the reaction decreases) in the order proto, meso, deutero. (c) A marked pH dependence of both ligand affinity and cooperativity is maintained in the reconstituted Hb's IV: at pH 6 the fractional saturation with oxygen in air (Root effect) is lower for proto- than for meso- and deutero-Hb IV. The results obtained, including partial photodissociation experiments at different pH values, can be considered, to a first approximation, consistent with the basic features of a simple two-states model.

Allosteric Regulation↗
PubMed1978

Effect of drugs on oxidation and precipitation of the isolated chains of human hemoglobin.

The paper deals with the action of: primaquine, epinephrine, adrenochrome, acetylphenylhydrazine and sulphanilamide on the autoxidation of the isolated chains from human hemoglobin and on the precipitation which follows. The effect of superoxide dismutase and catalase on the drug induced autoxidation allows the assessment of the possible role of O2 derivatives (notably superoxide or peroxide) in the overall reaction mechanism. It is also shown that primaquine and acetylphenylhydrazine enhance precipitation of the isolated oxidized chains, while epinephrine and adrenochrome display a small inhibitory effect on precipitation. These effects do not involve O2 radicals, but have presumably to be related to a destabilizing (or stabilizing) action of the drugs on the structure of the protein.

Adrenochrome↗
PubMed1975

Bakers' yeast uridine nucleosidase. Purification, composition, and physical and enzymatic properties.

Uridine nucleosidase (EC 3.2.2.3) was purified from commercial bakers' yeast to homogeneity, as judged by a single band observed on polyacrylamide disc gel electrophoresis. The molecular weight of the enzyme, estimated by gel filtration, was approximately 32,500. Polyacrylamide electrophoresis in 0.2% sodium dodecyl sulfate showed the presence of two apparently identical subunits of 17,000 molecular weight. The amino acid composition indicated a large excess of glutamic acid and aspartic acid over other amino acid residues and a very low content of tyrosine and tryptophan. Th SH groups analysis performed with 5,5'-dithiobis (2-nitrobenzoic acid) on thenative protein as well as in the presence of 1% sodium dodecyl sulfate showed the existence of one sulfhydryl group per mole of enzyme. Uridine nucleosidase is active on uridine and 5-methyluridine (ribosylthymine) resulting inactive toward all other pyrimidine and purine nucleosides tested. The Km values for uridine and 5-methyluridine were 0.86 x 10(-3) M and 1.66x10--3M, respectively. The optimal pH is around 7.0. The isoelectric point is 5.1. Among a variety of compounds tested only ribose and glucose 6-phosphate were inhibitory and Ki values were 7.2 mM and 0.19 mM, respectively. Furthermore, ribosylthymine competitively inhibited the hydrolysis of uridine. The type of all inhibitions was competitive and the n' values of the Hill plots were near 1. The effect of temperature on the enzyme activity plotted accoring to Arrhenius gave a value of E = 4740 cal per mole. The enzyme in 100 mM phosphate, pH = 7.0, is stable at 4 degrees for 15 days without any loss of activity.

Amino Acids↗
PubMedDate not supplied

Bovine pancreatic trypsin inhibitor and homologous polypeptide inhibitors in nephron cells.

Bovine pancreatic trypsin inhibitor (BPTI, aprotinin) is a fifty-eight amino acid polypeptide, which is present together with related molecular isoforms in various bovine organs. In the present study these protease inhibitors were isolated from bovine kidney by affinity chromatography on immobilized trypsin and a subsequent FPLC step. Due to their electrophoretic, structural, and inhibitory properties, the inhibitors were strictly similar to the polypeptides identified previously in other bovine organs. Immunohistochemical experiments showed a widespread localization of these polypeptides in nephron epithelial cells (proximal and distal tubules, loop of Henle, collecting tubules).

Amino Acid Sequence↗