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Biomedical subjects

E Marinello

Publications and source records attributed to E Marinello.

At least 109 records · Page 6Linked to original sources
PubMed1992

Levels and variability of purine nucleotides in normal human lymphocytes.

Anion-exchange, high performance liquid chromatography was used to determine purine nucleotides in lymphocytes of healthy males and females of various ages. We observed a considerable dispersion of values which were unrelated to age or sex, possibly linked to various states of activation of circulating lymphocytes and to other unknown factors.

Adult↗
PubMed1991

High-performance liquid chromatography of thiazolidinic compounds obtained by condensation of pyridoxal 5'-phosphate or pyridoxal with aminothiols (L- or D-cysteine, cysteamine, L-cysteine ethyl ester).

We investigated six thiazolidine 4-carboxylic acids of biological interest, obtained by condensation of pyridoxal 5'-phosphate or pyridoxal with L- or D-cysteine, cysteamine or L-cysteine ethyl ester. A reversed-phase high-performance liquid chromatographic method, using a C18 column for their separation, was developed by sequential optimization of the pH and the gradient of the mobile phase. Resolution of the compounds was obtained with an analysis time of less than 20 min.

Chromatography, High Pressure Liquid↗
PubMed1991

Some aspects of purine nucleotide metabolism in lymphocytes of B-CLL.

The authors studied the behavior of some enzymes involved in purine nucleotide metabolism in human peripheral blood lymphocytes from normal and B-cell chronic lymphocytic leukemia subjects. Determinations were made with radiochemical methods associated with high performance liquid chromatography. Results indicated a marked increase in de novo purine synthesis enzymes, particularly those of the "inosinic branch point". The latter were absent in normal lymphocytes, whereas they were well evident in leukemic lymphocytes, with the exception of AMP-S synthetase. Whereas the enzymes of the "salvage pathway" were spared in comparison to other proteins, those of the "catabolic pathway" significantly decreased. The authors discuss the possibility that such enzymes may be used as tumor markers.

AMP Deaminase↗
PubMed1991

The inhibition of rat liver threonine dehydratase by carbamoyl-phosphate. The formation of carbamoylpyridoxal 5'-phosphate.

The effects exerted by carbamoyl phosphate (CP) and cyanate (KCNO) on rat liver L-threonine deaminase have been studied. The two compounds showed that same effects, inhibiting through a competitive mechanism both the holoenzyme and the dialyzed enzyme; inhibition was more evident for the latter. Ki values, both for L-threonine and pyridoxal 5'-phosphate (PLP), were lower for the apoenzyme and the inhibitors also affected the Km of the apoenzyme for PLP. The effects of CP and KCNO are mainly due to an interference in the association reaction apoenzyme + PLP in equilibrium holoenzyme This was clearly demonstrated by the fact that, when PLP was incubated with CP or KCNO, it failed to enhance the activity of the holoenzyme nor did it reactivate the resolved apoenzyme. Such interference of CP and KCNO in the L-threonine deaminase activity was mainly due to a specific mechanism, the formation of a new derivative of PLP. The reaction of PLP with either CP or KCNO occurred readily, at low concentrations, under physiological conditions. The new compound was identified as 3,4-dihydro-2H-pyrido[3,4-e]1,3-oxazin-2-one derivative by ultraviolet-visible spectra, elemental analysis, infrared, NMR and MS spectra. In this paper we formulate the hypothesis that this compound is involved in the regulation of the CP and PLP intracellular content and in the control of PLP dependent enzymes.

Animals↗