Search PubMed⌕ Search

Biomedical subjects

A Morello

Publications and source records attributed to A Morello.

At least 55 records · Page 3Linked to original sources
PubMed1983

Trypanosoma cruzi: carboxylesterase activity in intact epimastigotes.

Carboxylesterase activity corresponding to types A and B has been demonstrated in intact T. cruzi epimastigotes as shown by the hydrolysis of several esters of p-nitrophenol and the effect of suitable inhibitors. The in situ carboxylesterase activity was described by the Michaelis Menten kinetic approach. The apparent Vmax for the acetate and butyrate esters were 66.5 and 165.3 nmol hydrolysed per min and mg of protein respectively. An Arrhenius plot of the temperature dependent activity showed two sharp linear regions with a transition temperature of 31.6 degrees C. and energies of activation of 6.2 and 14.1 kcal/mol. The in situ carboxylesterase activity was inhibited 26% by paraoxon and 56% by N-ethylmaleimide, but not by p-chloromercuribenzoate.

Animals↗
PubMed1983

In vitro and in vivo studies of Trypanosoma cruzi DNA polymerase.

One major DNA polymerase has been purified and characterized from Trypanosoma cruzi. The enzyme has a sedimentation coefficient of 6.8 S corresponding to an approximate molecular weight of 180,000 assuming a globular shape. The enzyme recognizes activated DNA very efficiently, as well as synthetic polydeoxynucleotides, whereas poly rA-dT12 is very poorly utilized. Trypanosoma cruzi DNA polymerase is not inhibited at all by aphidicolin, while araCTP inhibits the enzyme very slightly. The purified enzyme is strongly inhibited by N-ethyl maleimide, dideoxyTTP, ethidium bromide and berenil. All our attempts to find a DNA polymerase sensitive to aphidicolin in vitro have failed, nor have we been able to find a low molecular weight DNA polymerase in this organism. However, when DNA synthesis was studied in whole trypanosomes, aphidicolin was shown to inhibit DNA synthesis more efficiently than ethidium bromide and berenil.

Animals↗
PubMed1982

Characterization of glutathione S-transferase activity in Echinococcus granulosus.

1. Glutathione S-transferase activity has been characterized in protoscolices of Echinococcus granulosus. 2. The conjugation reaction was activated by treatment of protoscolices with phenobarbital and beta-naphthoflavone. 3. Protoscolices of E. granulosus contained the conjugation cofactor glutathione in the amount of 287 nmol/g fresh tissue. 4. Conjugation may represent an important factor in the resistance of the parasite to drugs.

Animals↗
PubMed1979

UDP-glucosyltransferase activity of housefly microsomal fraction.

Housefly UDP-glucosyltransferase activity towards p-nitrophenol was demonstrated in a system in vitro. The activity is localized in the microsomal fraction, requires UDP-glucose, is slightly stimulated by Mg2+ and is activated optimally over a wide range of detergent concentration. Phenobarbital increases the enzyme(s) activity about 3-fold, with p-nitrophenol as substrate, which differs from the corresponding mammalian glucuronyltransferase.

Animals↗
PubMed1979

Fate of juvenile hormone in mammalian cell culture.

The metabolism of juvenile hormone (JH) I has been examined in fetal mouse liver cells maintained in culture. Diffusion of the hormone into the cells appears to be passive. The hormone is metabolized essentially to organic-soluble metabolites (diol ester, diol acid and acid) by the action of epoxide hydrase and carboxylesterases. Conjugative reactions play a minor role, less than 3% of the hormone being excreted as conjugates (glucuronides, sulfates and mercapturic acid). About 0.8% of the cellular radioactivity is bound to macromolecules, mainly those of nuclear and mitochondrial origin. Metyrapone and SKF 525-A inhibit covalent binding of the hormone to cytoplasmic macromolecules, which suggests participation of the cytochrome P-450 system in covalent binding of the hormone.

Animals↗
PubMed1971

Cytochrome P-450 and hydroxylating activity of microsomal preparations from whole houseflies.

1. A new microsomal preparation, obtained from whole houseflies is described in terms of its cytochrome P-450 content and its hydroxylating activity. 2. Microsomes prepared from whole-fly brei, obtained with the aid of a mortar (a procedure that avoids the destruction of sarcosomes), contain 0.265nmol of cytochrome P-450 and hydroxylate naphthalene at a rate of 28.5nmol/mg of microsomal protein in 30min at 30 degrees C. This corresponds to 104nmol of naphthalene hydroxylated/nmol of cytochrome P-450. This is the highest rate ever reported for housefly and rat liver microsomal preparations. 3. Microsomal fractions prepared by procedures that do not retain the integrity of sarcosomes show the presence in the CO-difference spectrum of a 428nm peak. This cytochrome is associated with sarcosomal microsomes and it may be involved in the inhibition of insect microsomal mixed-function oxidases, although other factors cannot be discarded at present. 4. The inability to show cytochrome P-450 in microsomal fractions isolated from whole houseflies by other procedures may be at least partially due to a masking effect brought about by contamination with the sarcosomal cytochrome.

Animals↗