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1.
Dokl Biol Sci ; 492(1): 99-102, 2020 May.
Article in English | MEDLINE | ID: mdl-32632836

ABSTRACT

The dynamics of body temperature was used to determine the food intake synchronization in starlings located at a distance of 105 km from each other. Thermal accumulators were implanted intraperitoneally to the birds; the birds had free access to food or were kept under the conditions of food deprivation. It was found that food intake moments significantly more often coincided with an accuracy of up to a minute even in the birds separated by a considerable distance. The difference in time of sunrise of a few minutes, as well as the conditions of constant lighting did not affect the synchronism of food intake. On the basis of the data obtained, it can be assumed that there is a certain external factor, probably of an electromagnetic nature, which synchronizes the functional activity of the body, including food intake.


Subject(s)
Body Weight/physiology , Eating/physiology , Starlings/physiology , Animals , Body Temperature/physiology , Circadian Rhythm/physiology , Lighting
2.
Bull Exp Biol Med ; 168(2): 291-294, 2019 Dec.
Article in English | MEDLINE | ID: mdl-31782004

ABSTRACT

The rhythms of short-term arousal episodes, associated with normalization of low body temperature, were studied in hibernating Erinaceus roumanicus. The episodes of body temperature recovery during hibernation were 1.7 times more incident during the acrophase of 4.058-day rhythm of glucocorticoid hormones, detected previously, than during the batiphase of this rhythm. Ultradian rhythm of arousal episodes conformed to a 4-h biorhythm: the maximum number of body temperature resumption episodes was recorded at 00.00-01.00, 04.00-05.00, 08.00-09.00, 12.00-13.00, 16.00-17.00, and 20.00-21.00. These data indicated that in mammals the mechanisms of infradian and ultradian rhythm maintenance were stable and did not depend on body temperature or were determined by external factors with periods of 4.058 days and 4 h.


Subject(s)
Body Temperature/physiology , Circadian Rhythm/physiology , Hedgehogs/physiology , Hibernation/physiology , Infradian Rhythm/physiology , Ultradian Rhythm/physiology , Animals , Biological Clocks/physiology , Seasons
3.
Mol Biol (Mosk) ; 51(6): 985-996, 2017.
Article in Russian | MEDLINE | ID: mdl-29271962

ABSTRACT

A new efficient method for the parallel and sequential stepwise generation of single-domain antibodies to various high-abundance human-plasma proteins has been described. Single-domain antibodies have a number of features that favorably distinguish them from classical antibodies. In particular, they are able to recognize unusual unique conformational epitopes of native target proteins, small in size, and relatively easily produced and modified; have enhanced stability; and rapidly renature after denaturation. As a consequence, the immunosorbents that utilize these antibodies can be reused without any significant loss of activity. The principal novelty and universality of the described method is that it enables the sequential generation of antibodies to a number of high-abundance and yet unknown antigens of a complex protein mixture without the need for purified antigens. The effectiveness of the method is demonstrated by the example of generation of single-domain antibodies to a number of high-abundance proteins of the human blood plasma. The produced antibodies are promising biotechnological tools that can be used to develop prototypes for new diagnostic and therapeutic agents, as well as appropriate immunoaffinity-based methods for removal, enrichment, analysis, and/or targeting of specified proteins and their complexes from (in) the human blood. As we show, the generated single-domain antibodies can be efficiently used in designing new immunosorbents. As a rule, commercially available analogous immunosorbents that utilize classical antibodies remove many major proteins from the blood plasma immediately, while immunosorbents for many individual proteins are difficult to find and rather expensive. Single-domain antibodies generated by our method are unique new materials that allow for the development of more efficient and delicate approaches to pretreatment of plasma and the analysis of various blood plasma biomarkers.


Subject(s)
Blood Proteins/isolation & purification , Chromatography, Affinity/methods , Immunosorbent Techniques , Proteomics/methods , Single-Domain Antibodies/metabolism , Animals , Blood Proteins/chemistry , Blood Proteins/immunology , Camelus , Cloning, Molecular , Epitopes/chemistry , Epitopes/immunology , Gene Expression , Humans , Protein Stability , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Single-Domain Antibodies/chemistry , Single-Domain Antibodies/genetics
4.
Biomed Khim ; 63(5): 461-466, 2017 Oct.
Article in Russian | MEDLINE | ID: mdl-29080882

ABSTRACT

The technology for the generating of single-domain recombinant monoclonal antibodies (nanoantibodies) based on the immunization of a camel, cloning of induced sequences encoding single-domain antigen-recognizing fragments of non-canonical camel antibodies, as well as functional selection of clones of nanoantibodies by the phage display method, was used to obtain new effective tools for more efficient diagnostics of Chlamydia infection and to develop new approaches for effective therapy. Two promising nanoantibodies were obtained. They showed effective binding to extracellular and intracellular forms of C. trachomatis, and also had activity that inhibited the development of chlamydial infection in vitro.


Subject(s)
Antibodies, Bacterial/immunology , Antibodies, Monoclonal/immunology , Chlamydia Infections/immunology , Chlamydia trachomatis/immunology , Single-Domain Antibodies/immunology , Animals , Camelus , Immunization
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