Biopolym. Cell. 1990; 6(3):59-65.
Структура та функції біополімерів
Вплив іонної сили
на ферментативну активність тромбіну
- Інститут біоорганічної хімії та нафтохімії АН УРСР
Київ, СРСР
Abstract
Досліджено вплив іонної сили середовища на активність тромбіну (TP) за дії його на фібриноген (ФГ) і низькомолекулярний субстрат. Зроблено висновок про те, що умови низької іонної сили (І = 0,05–0,07) є сприятливими для специфічної взаємодії TP з ФГ, яка не зачіпає активного центра ферменту.
Повний текст: (PDF, російською)
References
[1]
Fenton JW 2nd. Regulation of thrombin generation and functions. Semin Thromb Hemost. 1988;14(3):234-40.
[2]
Seegers WH, Hassouna HI, Hewett-Emmett D, et al. Pro- thrombin and thrombin: selected aspects of thrombin formation, properties, inhibition, and immunology. Semin Thromb Hemost. 1975; 1:211-283.
[3]
Strukova SM, Sereyskaya AA. On the two types of the thrombin high molecular substrates. Thromb Res. 1988;49(2):303-4.
[4]
Strukova SM, Sereyskaya AA, Osadchuk TV. Structural basis of specificity of thrombin. Usp Sovrem Biol. 1989; 107(1):41-54.
[5]
Rotoli B, Ogunsawno B, Scarpato N. Optimizing and stabilizing thrombin activity. Haematologica. 1986;71(6):463-6.
[6]
Pozdnyakova TM. The mechanism of self-assembly of fibrin. Biokhimiya zhivotnykh i cheloveka. 1989; (13):27-36.
[7]
Landis BH, Koehler KA, Fenton JW 2nd. Human thrombins. Group IA and IIA salt-dependent properties of alpha-thrombin. J Biol Chem. 1981;256(9):4604-10.
[8]
Hantgan RR, Hermans J. Assembly of fibrin. A light scattering study. J Biol Chem. 1979;254(22):11272-81.
[9]
Varetskaya TV. Structure and properties of fibrinogen and fibrin. Self-assembly of fibrin fibers: Author. dis. ... Dr. biol. nauk. Kyiv, 1977; 40 p.
[10]
Keil B. Trypsin. The enzymes. Ed. P. D. Boyer. New York: Acad, press, 1971. Vol. 3:249-275.
[11]
Roberts PS, Hughes HN, Fleming PB. The effects of hepes buffer on clotting tests, assay of factors V and VIII and on the hydrolysis of esters by thrombin and thrombokinase. Thromb Haemost. 1976;35(1):202-10.
[12]
Fenton JW, Landis BH, Walz DA et al. Human thrombin: Preparative evaluation, structural properties, and enzymic specificity. Chemistry and physioiogy of human plasma proteins. Ed. D. H. Bing. New York: Pergamon press, 1979:151-173.
[13]
Varetskaya TV. Microheterogeneity fibrinogen: cryofibrinogen. Ukr Biokhim Zh. 1960; 32(1):13-27.
[14]
Varetskaia TV. Preparation of a fibrin monomer and studies on some of its properties. Ukr Biokhim Zh. 1965;37(2):194-206.
[15]
Fenton JW 2nd, Fasco MJ, Stackrow AB. Human thrombins. Production, evaluation, and properties of alpha-thrombin. J Biol Chem. 1977;252(11):3587-98.
[16]
Lewis SD, Shafer JA. A thrombin assay based upon the release of fibrinopeptide A from fibrinogen: definition of a new thrombin unit. Thromb Res. 1984;35(2):111-20.
[17]
Steven FS, Griffin MM. Inhibition of thrombin cleavage of fibrinogen by polyestradiol phosphate; interaction with the crucial arginine residues in fibrinogen required for enzymic cleavage. Int J Biochem. 1982;14(8):699-700.
[18]
Fasco MJ, Fenton JW. Specificity of thrombin. I. Esterolytic properties of thrombin with derivatives of pNPGB. Arch Biochem Biophys. 1973;159(2):802–12.
[19]
Kull FJ, Vellekamp GJ, Button EE. Ionic strengths and enzyme activities. Trends Biochem Sci. 1982;7(9):317–8.
[20]
Alekseenko LP. Methods for determining of the proteolytic enzymes activity. Modern methods in biochemistry. Moscow, Medicine, 1977; 119-20.
[21]
Belitser VA, Varetskaja TV, Malneva GV. Fibrinogen-fibrin interaction. Biochim Biophys Acta. 1968;154(2):367-75.
