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N A Matveeva

Publications and source records attributed to N A Matveeva.

At least 19 recordsLinked to original sources
PubMed2004

The influence of cryoglobulins on the temperature-dependent erythrocyte aggregation in vitro by backscattering nephelometry.

Nephelometry technique was used to register the alterations of the scattering signal from a whole blood sample due to erythrocyte aggregates in stasis and under controlled shear stress. The measured parameters were: the characteristic times of linear and three-dimensional aggregates formation, and the strength of aggregates of different types. These parameters depend on the sample temperature in the range of 2/50 degrees C. Temporal parameters of the aggregation process strongly increase (by 3 times) at temperature 45 degrees C. For samples of normal blood the aggregates strength parameters do not significantly depend on the sample temperature, whereas for blood samples from patients with cryoglobulinemia high increase of the strength of both three-dimensional and linear aggregates and decrease of time of linear aggregates formation at low temperature of the sample (4 degrees C) was observed. The difference of these parameters of the pathological blood from that of the normal at room temperature was quite opposite. Possible reasons of such behavior of aggregation state of blood and explanation of the observed effects are suggested.

Cryoglobulinemia↗
PubMed1986

[Regulation of the orientation of the IgG and IgM molecule at the interface].

Pathological immunoglobulins (IgG from patients with multiple myeloma and IgM from patients with Waldenström macroglobulinemia) have been shown to possess hydrophylic-lipophylic balance (HLB) which differed from normal Ig HLB. HLB deficiency in pathological proteins was due to the increase of hydrophobic area at the surface of protein globe, which was the reason for different normal and abnormal Ig orientations at the aqueous NaCl solution--air interface. The normal IgG and IgM had horizontal orientation while abnormal ones had vertical orientation. Both normal and abnormal Ig changed their orientation in monolayers as a result of sodium deoxycholate processing. The change in orientation depended on protein molecules interaction with single molecules or micelles of sodium deoxycholate.

Chemical Phenomena↗
PubMed1984

[Identical nature of the differences between normal and myeloma IgG in the mouse and man determined by the monolayer method].

The surface denaturation kinetics of mouse normal IgG and IgGl kappa secreted by myeloma MOPC-21 was studied in monomolecular layers at the air-water interface. Based on the denaturation kinetics data the orientation of the native IgG molecules was determined relative to the interface surface, which turned out to be horizontal for normal IgG and vertical for myelomic ones. As regards the orientation in the monolayers and the rate of surface denaturation, the mouse normal IgG were found to be similar to normal IgG from other species. Like human myelomic IgG, MOPC-21 IgGl kappa differed from normal IgG in both the orientation and lesser native structure stability.

Animals↗