An improvement to the purification method for human salivary peroxidase is presented. The enzyme is obtained at a higher degree of purity in two chromatographic steps instead of four, and avoiding lyophilation treatment. Differences in electrophoretic pattern confirm the genetic polymorphism of the peroxidase of human saliva.

Electrophoresis, Polyacrylamide Gel↗

PubMedDate not supplied

A simple method for the purification of type 1 RIPs.

We describe a straightforward and simple method for obtaining pure and active preparations of type 1 ribosome inactivating proteins (RIPs). The very high isoelectric point values, characteristic of these proteins, allow this purification in a single chromatographic step.

Chromatography, Ion Exchange↗

PubMedDate not supplied

Effects of surfactants on the stabilization of the bovine lactoperoxidase activity.

Bovine lactoperoxidase (LPO) is taken as a model protein of mammalian peroxidases to investigate the activity and the stability of the enzyme in the presence of different surfactants. The cationic benzalkonium chloride (Bz) has proved efficient in preserving the enzymatic activity for over 10 days, while the native enzyme completely lost its activity within 3-4 days. The presence of Bz allows the enzyme to preserve its secondary structure for a long time, as shown in CD spectra, and creates a more hydrophobic environment for the enzyme, as indicated in fluorescence studies. Moreover, this surfactant at a concentration of 0.01% (0.3 mM) increases the lactoperoxidase activity in the first 2 h of incubation at 37 degrees C. Both hydrophobic and electrostatic interactions of the cationic surfactant seem to be responsible for the enzyme activation and stabilization, and this is a promising result in view of industrial applications of enzymes.

Animals↗

PubMedDate not supplied

Variations of lacrimal fluid peroxidase activity in female and male rats.

Previous research from this laboratory showed that human lacrimal fluid peroxidase has cyclic variations during the menstrual cycle, correlated with plasma levels of 17beta-oestradiol. In the present investigation, variations of enzyme activity and total protein content during the oestrous cycle of young adult female rats are analysed. Effects from circadian rhythm and a gender-related influence are also examined. In female rats, as in women, lacrimal fluid peroxidase activity shows cyclic variations; in fact, it significantly (p < 0.05) changes during the different phases of the oestrous cycle. In contrast, in males such variations do not occur. Thus, we suggest that gender seems to exert a significant influence on the secretion of this specific tear protein, probably by a direct effect of oestrogens.

Animals↗

PubMedDate not supplied

Effect of oral contraceptives on lacrimal fluid peroxidase activity in women.

Lacrimal fluid peroxidase has been supposed to be involved in the protection against oxidative damage to the ocular surface. Our recent findings showed the existence of significant cyclic variations in lacrimal fluid peroxidase activity that were positively correlated with those of 17beta-estradiol plasma levels throughout the menstrual cycle of fertile women. In the present study lacrimal fluid peroxidase activity of 8 healthy normocyclic women using low-dose oral contraceptives during the monthly cycle was determined. Data showed that low-dose oral contraceptives caused a decrease in lacrimal fluid peroxidase activity and a lack of its cyclic pattern with respect to the enzyme activity of 8 untreated age-matched women. Moreover, this result suggests that lacrimal fluid peroxidase activity could be regulated by estrogen.

Adult↗

PubMedDate not supplied

[Use of digestive peroperative endoscopy in syndromes of difficult diagnosis].

Explore the source record for details and available documents.

Diagnostic Techniques, Surgical↗