Glycoprotein composition of olfactory mucus in vertebrates.

Acid water-soluble glycoproteins of olfactory mucus in various representatives of the vertebrate have been studied. Olfactory mucus of these representatives is found to be of great similarity in its glycoprotein composition. The universal presence of these glycoprotein components of the mucus is supposed to testify to their similar functional significance in various vertebrates.

[Possible apical respiration in the olfactory epithelium of the frog Rana temporaria].

Bioluminescent analysis has been made of the effect of oxygen supply on the content of ATP in the isolated olfactory epithelium of the frog. It was shown that storage of epithelium preparations in the air increases their ATP content. When preparations are kept in the atmosphere of an inert gas, ATP level in the epithelium rapidly decreases, being recovered after transition of preparations to the air medium.

[ATP in the frog olfactory organ].

The distribution of ATP in different parts of the frog olfactory organ was investigated. It is demonstrated that the highest macroerg amount is characteristic of the receptor part of olfactory mucosa. The amount of ATP decreased after the stimulation of the olfactory mucosa by odorants.

[Water-soluble proteins of Pacinian corpuscles].

The composition of water soluble proteins has been investigated in different parts of Pacinian corpuscles. The Pacinian corpuscles fluid proteins have been compared with the receptor homogenate proteins and blood serum of a cat. It is supposed that proteins of the Pacinian corpuscle fluid are produced from the blood system on the whole.

[Characteristics of lactate dehydrogenase isoenzyme distribution in Pacinian corpuscles].

The paper deals with the isoenzymic LDG composition in different sections of Pacinian corpuscles. It is found that intracapsular liquid has the aerobic LDG spectrum. The stromal part of the receptor including lamellar capsule structures, inner cone and nerve endings has the anaerobic LDG spectrum.

[Alkaline phosphomonohydrolases of Pacinian corpuscles].

Research on quantitative determination of activity of alkaline phosphatase (EC) 3.1.3.

[Alkaline phosphatase properties of the olfactory lining of the bull].

Biochemical and electrophoretic characteristics of enzyme alkaline phosphatase and its localization in the bull's olfactory mucose structures have been investigated. The activity of enzymes was found to change with odour stimulation. Using electron microscope histochemistry a considerable activity of this enzyme has been demonstrated in the structures secreting olfactory mucus, and in the mucus itself, with alkaline phosphatase macromolecules being concentrated on the surface membrane of olfactory cilia, forming a layer around these.

[Properties of the olfactorymucosa's water-soluble proteins].

A quantitative and qualitative biochemical investigation was carried out for the composition of water-soluble proteins in preparation of the bull's olfactory mucosa scrape. Comparing the results with those obtained for a similar preparation of a nonsensory nature (a preparation of a respiratory epithelium scrape) the authors found that the most electrically-mobile protein fractions differ in their physical properties and number. A reaction for glycoproteins showed that with an alcian blue an appropriate colour for acidic glycoproteins is given only by two protein fractions.

[Magnesium-activated adenosine triphosphate of the ampullae of Lorenzini of the skate Dasyatis pastinaca].

Studies have been made on Mg2+-activated ATPase of electroreceptor structures of the lateral line organin the ray D. pastinaca. It was shown that the enzyme is activated by magnesium ions (2.

[Mg, Ca-activated ATP-ase of Pacinian corpuscles].

Adenosine triphosphatase (ATPase) activated by Mg2+ or Ca2+ ions was detected in single mechanoreceptors (Pacini's corpuscles) of cat; addition of Ca2+ (10(-5)M) to Mg-ATP-ase increased the activity by the factor of 1.6. The activity optimum of Mg- or Co-ATPase was in the alkaline pH zone.