[Thymosin alpha(1)–an endogenous modulator of alpha-thrombin recognition site]статья

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Дата последнего поиска статьи во внешних источниках: 11 декабря 2012 г.

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[1] [thymosin alpha(1)–an endogenous modulator of alpha-thrombin recognition site] / T. N. Dugina, S. M. Strukova, S. V. Khlgatian, I. P. Ashmarin // Biulleten' eksperimental'no∎ biologii i meditsiny. — 1992. — Vol. 114, no. 9. — P. 260–2. Thymosin alpha 1-inhibited fibrinogen clotting activity of alpha-thrombin, but not amidolysis of H-D-Phe-Pip-Arg-pNA. Modulation of thrombin interaction with rat peritoneal mast cells (RPMC) by suppressors of additional recognition binding site (thymosin and heparin) was studied. Thrombin-induced pHi changes of RPMC were controlled with pH-sensitive fluorescent dye, BCECF. Thrombin caused a biphasic changes in pHi: rapid cell acidification (0.02) followed by slow alkalinization (0.06 above baseline for 18 min). Thymosin suppressed thrombin-induced pHi increase above resting level. Similar changes in pHi were observed after modification of additional recognition binding site by heparin. Beta/gamma-thrombin with disrupted additional binding site was shown to induce only a decrease of pHi. It is concluded that thymosin alpha 1 is endogenous modulator of alpha-thrombin activity.

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