[Morphology and diagnosis of the oral protozoans Trichomonas tenax and Entamoeba gingivalis using the Giemsa-Romanovsky stain].

In the microscopic diagnosis of Trichomonas tenax and Entamoeba gingivalis is the technically and time not demanding native preparation of a culture, in which both protozoans can be detected according to their typical motility, determining. In the permanent preparation of the culture stained according to Giemsa-Romanovsky, which has also documentary character, are all of the characteristic cell organelles stainable, enabling so their detection without their typical motility. Staining according to Giemsa-Romanovsky is technically simple and not time consuming, not very laborious, low cost and the coloration is permanent, that means optimal for the diagnostic of oral protozoans in permanent preparations.

Selective oxidation of methionyl residues in the human recombinant secretory leukocyte proteinase inhibitor. Effect on the inhibitor binding properties.

Binding of the human recombinant secretory leukocyte proteinase inhibitor (SLPI) [native and with the methionyl residues at positions 73, 82, 94 and 96 of domain 2 oxidized to the sulfoxide derivative (Met(O) SLPI)] to bovine alpha-chymotrypsin (alpha-chymotrypsin) [native and with the Met192 residue converted to the sulfoxide derivative (Met(O) alpha-chymotrypsin)] as well as to native bovine beta-trypsin (beta-trypsin), which does not contain methionyl residues, has been investigated between pH 4.0 and 8.0, and between 10.

Selective oxidation of Met-192 in bovine alpha-chymotrypsin. Effect on catalytic and inhibitor binding properties.

Catalytic and inhibitor binding properties of bovine alpha-chymotrypsin, in which the Met-192 residue has been converted by treatment with chloramine T to the sulfoxide derivative (Met(O)192 alpha-chymotrypsin), have been examined relative to the native enzyme (alpha-chymotrypsin), between pH 4.5 and 8.0 (mu = 0.

Hemoglobin Dallas (alpha 97(G4)Asn-->Lys): functional characterization of a high oxygen affinity natural mutant.

Hemoglobin Dallas, an alpha-chain variant with a substitution of lysine for asparagine at position 97(G4), was found to have increased oxygen affinity (p1/2 = 1 mmHg at pH 7.3 and 20 degrees C), diminished cooperativity (n, the Hill coefficient = 1.7) and reduced Bohr effect (about 50%).

[Occurrence of the protozoa, Entamoeba gingivalis and Trichomonas tenax in the mouths of children and adolescents with hyperplastic gingivitis caused by phenytoin].

The oral protozoa Entamoeba gingivalis and Trichomonas tenax do not occur in small children and are rarely found in older ones. In adolescents their occurrence rate keeps increasing with age. They parasitize in an oral cavity changed by inflammation, yet also in a healthy mouth.

[Morphology and diagnosis of Entamoeba gingivalis and Trichomonas tenax and their occurrence in children and adolescents].

Specimens obtained from 176 eight- to nineteen-year-old subjects were cultured for oral protozoa. Of the given series, 25 subjects (14.2%) had in their mouth only E.

Purification of the proteolytically solubilized, active catalytic subunit of adenylate cyclase from ram sperm. Inhibition by adenosine.

Ram spermatozoa adenylate cyclase is insensitive to all usual regulatory processes. The purification of its active catalytic subunit was accomplished after proteolytic solubilization of a particulate fraction by alpha-chymotrypsin. The purification (26,000-fold from the particulate fraction or 125,000-fold from the whole-sperm proteins) was achieved by conventional procedures (DEAE-Trisacryl, Ultrogel AcA 34, DEAE-Sephacel, hydroxyapatite), in the absence of detergent, and with a yield of 5-10% and a final specific activity of 19 mumol cyclic AMP formed mg protein-1 min-1 at 30 degrees C in the presence of manganese as cosubstrate.

Inhibition of the catalytic subunit of ram sperm adenylate cyclase by adenosine.

Adenosine inhibits ram sperm adenylate cyclase activity which is membrane-bound and comprises only the catalytic subunit. The inhibition parameters of adenylate cyclase by adenosine were not modified when the enzyme was purified 3 to 5,000 fold. Optimal inhibition by adenosine was found to require a high concentration of manganese, and exhibited a noncompetitive pattern up to a concentration of 1 mM adenosine.

Studies on the influence of ochratoxin A on rat lenses.

The influence of ochratoxin A on enzyme activities and on the content of free adenine nucleotides and intermediates of glycolysis in rat lenses was investigated. For a period of eight weeks, five times weekly, albino Wistat rats received ochratoxin A in 0.1% NaHCO3, dosed 1/100 LD50, via stomach tube.