[Immunological properties and biological activity of chicken glucagon]. 1987

I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia

A comparative study of avian (chicken) glucagon and commercial preparations of cattle glucagon was carried out with the view of studying the evolution of polypeptide hormones in some vertebrate species. A chromatographic procedure for obtaining crystalline hormone preparations from chicken tissues was developed. Study of immunological properties of chicken glucagon in radioimmune systems with highly specific antisera to mammalian glucagon revealed that the immunoreactivity of chicken hormone preparations purchased from CNR (USA) and RSL (USA) makes up to 40% and 60% of that of mammalian glucagon. Estimation of biological activity of the hormones by their ability to activate adenylate cyclase in a test system with plasma membranes of chicken and rat liver as well as to stimulate lipolysis in a test system with chicken adipocytes revealed that chicken glucagon possesses a biological activity within the same concentration range as its mammalian counterpart, i. e., 2.9 X 10(-10)-1 X 10(-5) M. In the majority of cases the effect of chicken glucagon taken in the above concentrations was less pronounced than that of the mammalian hormone. The data obtained suggest that even one amino acid substitution in the chicken glucagon molecule (in comparison with mammalian glucagon) affects the immunological properties of the hormone and its biological activity.

UI MeSH Term Description Entries
D008066 Lipolysis The metabolic process of breaking down LIPIDS to release FREE FATTY ACIDS, the major oxidative fuel for the body. Lipolysis may involve dietary lipids in the DIGESTIVE TRACT, circulating lipids in the BLOOD, and stored lipids in the ADIPOSE TISSUE or the LIVER. A number of enzymes are involved in such lipid hydrolysis, such as LIPASE and LIPOPROTEIN LIPASE from various tissues. Lipolyses
D011863 Radioimmunoassay Classic quantitative assay for detection of antigen-antibody reactions using a radioactively labeled substance (radioligand) either directly or indirectly to measure the binding of the unlabeled substance to a specific antibody or other receptor system. Non-immunogenic substances (e.g., haptens) can be measured if coupled to larger carrier proteins (e.g., bovine gamma-globulin or human serum albumin) capable of inducing antibody formation. Radioimmunoassays
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005934 Glucagon A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511) Glucagon (1-29),Glukagon,HG-Factor,Hyperglycemic-Glycogenolytic Factor,Proglucagon (33-61),HG Factor,Hyperglycemic Glycogenolytic Factor
D000262 Adenylyl Cyclases Enzymes of the lyase class that catalyze the formation of CYCLIC AMP and pyrophosphate from ATP. Adenyl Cyclase,Adenylate Cyclase,3',5'-cyclic AMP Synthetase,Adenylyl Cyclase,3',5' cyclic AMP Synthetase,AMP Synthetase, 3',5'-cyclic,Cyclase, Adenyl,Cyclase, Adenylate,Cyclase, Adenylyl,Cyclases, Adenylyl,Synthetase, 3',5'-cyclic AMP
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
October 1974, Israel journal of medical sciences,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
April 1969, Diabetologia,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
September 1991, Journal of neurochemistry,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
June 1967, Endocrinology,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
January 1966, Recent progress in hormone research,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
November 1976, Metabolism: clinical and experimental,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
April 1973, Canadian journal of physiology and pharmacology,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
July 1969, Postgraduate medical journal,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
January 1975, Pathologia et microbiologia,
I M Shchenkova, and M N Pertseva, and L V Dmitrenko, and D I Ostrovskiĭ, and L P Soltitskaia
May 1976, The Biochemical journal,
Copied contents to your clipboard!