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Biomedical subjects

D Cavallini

Publications and source records attributed to D Cavallini.

At least 127 records · Page 7Linked to original sources
PubMed1965

The role of sulphur, sulphide and reducible dyes in the enzymic oxidation of cysteamine to hypotaurine.

1. Cysteamine is oxidized to hypotaurine by an enzyme extracted from horse kidney, with sulphur or sulphide acting as a cofactor. It has been now found that, when the enzyme is omitted, sulphur and sulphide are able to catalyse the oxidation of cysteamine to cystamine by molecular oxygen. 2. Methylene blue may be used in catalytic amounts as a cofactor in the enzymic oxidation of cysteamine to hypotaurine in the place of sulphur or sulphide. The effect of methylene blue is not light-dependent and is not abolished by catalase. Other redox dyes with E'(0) higher than that of methylene blue are also used as cofactors. 3. A property common to all the cofactors is that they are necessary for the enzymic process in catalytic amounts, though they depress the final amount of hypotaurine produced when added over a critical concentration. All the cofactors share also the property of being catalysts for the non-enzymic oxidation of cysteamine to cystamine. 4. Methylene blue is reduced by cysteamine under anaerobic conditions, and is reoxidized in the presence of air. The rate of the reduction is not accelerated by the enzyme, indicating that the dye does not act in this reaction as a hydrogen carrier from the enzyme to oxygen. The possible mechanism of action of methylene blue and of the other cofactors is discussed.

Animals↗
PubMedDate not supplied

In vitro enzymatic conversion of pantothenylcysteine-4'-phosphate into cysteamine.

In vivo production of taurine can not proceed from cysteine via the action of cysteinsulphinic acid-decarboxylase in those mammalian organs where this enzymatic activity is absent, such as heart. The possibility of existence of another metabolic way is strengthened by the experimental finding that, in vitro, cysteamine is obtained from pantothenylcysteine-4'-phosphate through the combined action of two mammalian enzymes, i.e. pantothenylcysteine-4'-phosphate decarboxylase and pantetheinase, used in partially purified forms. This new route should be related to the known biosynthetic pathway of CoA.

Acid Phosphatase↗
PubMedDate not supplied

Oxidative deamination of S-aminopropylcysteine and S-aminoethylhomocysteine.

S-aminopropylcysteine and S-aminoethylhomocysteine are oxidized by snake venom L-amino acid oxidase in the presence of catalase with formation of the respective ketoderivatives. Only the ketoderivative of S-aminopropylcysteine cyclizes to give a seven membered ring (ketimine) absorbing at 296 nm. In the absence of catalase both ketoderivatives are oxidatively decarboxylated.

Amines↗
PubMedDate not supplied

Influence of diet on cystathionine ketimine and lanthionine ketimine content in human urine.

A simple HPLC procedure for the routine analyses of Cystathionine ketimine (CK) and Lanthionine ketimine (LK) content in human urine has been developed. The values obtained in morning urine of fifteen healthy subjects (both sexes, 25-45 years old) on a common mixed diet are 330-2480 micrograms/g creatinine (mean 1110) of CK and 100-420 micrograms/g creatinine (mean 200) of LK. Quantitation of the two ketimines in urine of subjects on strictly vegetarian diet indicate that while the excretion of LK is independent of the diet, the excretion of CK is significantly decreased in conditions of vegetarian diet.

Adult↗
PubMedDate not supplied

Detection and determination of cysteamine at the nanomole level.

Cysteamine determination is performed by using a coupled enzymatic system. The reaction product between cysteamine and bromopyruvate inhibits competitively and specifically D-amino acid oxidase activity. A reaction system allowing the quantitative assay of cysteamine at the nanomole level has been worked out. The standard curve is linear and the assay is useful in determining the cysteamine concentration in tissues and biological samples. The method is fast and of simple execution. The cysteamine concentration in several mammalian organs is also reported.

Amidohydrolases↗
PubMedDate not supplied

Studies of cyanolysis of the rhodanese-thionitrobenzoate complex.

The reaction of sulfur-free rhodanese with 5-5'-dithio-bis (2-nitrobenzoic acid) produces a modified enzyme with 35% of residual activity. The resulting enzyme derivative has 1.6 moles of thionitrobenzoate/mole of enzyme bound to sulfhydryl groups of rhodanese. Determination of free sulfhydryl groups of this derivative shows that during the reaction with 5-5'-dithio-bis (2-nitrobenzoic acid) oxidative formation of an intramolecular disulfide bridge between two sulfhydryl groups of rhodanese occurs. Cyanolysis of the modified enzyme produces an enzyme-thiocyano derivative which partially beta-eliminates with release of thiocyanate. The cleavage of disulfide bonds present in the enzyme-thionitrobenzoate adduct using labeled cyanide shows an incorporation of radioactivity in the protein higher than would be expected. An electrostatic bond between cyanide and positively charged groups of the enzyme is suggested. Most of bound cyanide is released when samples are acidified for protein hydrolysis. In these conditions the thiocyanoalanine residue cyclizes to form 2-iminothiazolidine-4-carboxylic acid.

Animals↗