Correlation of structure-dynamic properties and oxygen affinity lo haemoglobin's electrophoretic fractions of dolphiri-afaline Tursiops truncatus
DOI:
https://doi.org/10.7124/bc.0004E8Abstract
Intramolecular mobility of all fractions of haemoglobin in dolphin-afaline Tursiops truncatus has been studied by method of NMR-ralaxation. It has been determined that haemoglobin's fractions with more intramolecular mobility have more volume of hydrophobic cavities and smaller affinity to oxygen.References
Dudarev VP. Role of hemoglobin in the mechanisms of adaptation to hypoxia and hyperoxia. Kiev: Naukova Dumka, 1979; 150 p.
Starodub NF. Heterogeneous system of hemoglobin. Structural features, physico-chemical and functional properties of individual forms of hemoglobin and their role in the biochemical adaptation to the conditions of life. Usp Sovrem Biol. 1985; 99(3):385-400.
Lukyanenko VI, Vasilev AS, Lukyanenko VV. Heterogeneity and polymorphism of fish hemoglobin. ST-Peterburg: Nauka, 1991; 392 p.
Drabkin DL. A simplified technique for a large scale crystallization of human oxyhemoglobin; isomorphous transformations of hemoglobin and myoglobin in the crystalline state. Arch Biochem. 1949;21(1):224-32.
Davis BJ. Disc electrophoresis. II. Method and application to human serum proteins. Ann N Y Acad Sci. 1964;121:404-27.
Azhitski? GIu, Bagdasar'ian SN. [Possibility of isolation of monomeric immunochemically pure serum albumin]. Lab Delo. 1975;(12):712-4. PubMed
Vatman AA, Pronin IS. Nuclear magnetic relaxation and its application in chemical physics. M.: Nauka, 1979; 235 p.
Vatman AA, Pronin IS. Nuclear magnetic relaxation spectroscopy. M.: Energoatomizdat, 1986.
Aksenov SI. [Study of the dynamic structure of globular proteins using impulse methods of nuclear magnetic resonance]. Mol Biol (Mosk). 1983;17(3):475-83.
Fedotov VD. [Nuclear magnetic resonance and intramolecular mobility of proteins]. Mol Biol (Mosk). 1983;17(3):493-504.
Izmailova VYa, Rebinder PA. Pattern formation in protein systems. M.: Nauka, 1974; 329 p.
Shorokhov IuA. [Spectrophotometric method of determining oxyhemoglobin dissociation curves in a cuvette-desaturator]. Fiziol Zh SSSR Im I M Sechenova. 1974;60(4):654-6.
Kushakovskiy MS. Methemoglobinemia. Handbook of functional diagnostics. M.: Meditsina, 1970;423-7.
Ivannikov AI, Abramov VM, Volkov VIa, Zav'ialov VP. [Comparative investigation of the dynamic conformational properties of human myeloma immunoglobulin G of different subclasses using impulse NMR]. Mol Biol (Mosk). 1983;17(4):734-40.
Ostolovsky EM, Botsyansky AD, Zadorozniy BA. On intramolecular structure of mammalian serum albumin. Biofizika. 1990;35(5):762-4.
Konoshenko SV, Rakhman A. [The comparative characteristics of the physicochemical and structural-functional properties of hemoglobin in a number of vertebrates]. Zh Evol Biokhim Fiziol. 1994;30(5):683-9.
Berzhansky MK, Konoshenko SV, Kunevich AK, Ostolovsky EM. H-NMR-relaxation at T-R transition of haemoglobin. Proc XV Int conf magnetic resonance in biol. systems. Jerusalem, 1992;219.
Konoshenko SV. Structural and functional properties of hemoglobins in two reptiles species: Testudo horesfieldi and Natrix tesselata. Biopolym Cell. 1993; 9(6):49-52.
Konoshenko SV, Bayala Isso Comparison characteristic of intramolecular mobility and affinity to oxygen of hemoglobins in vertebrate line. Biopolym Cell. 1994; 10(2):72-8.
Peruts M. Mechanism of cooperativity and allosteric regulation in protein Nature. 1990; 347(6290):241-2