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The role of carbohydrate side chains of plasminogen in its activation by staphylokinaseстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Aisina R.B., Moukhametova L.I., Gershkovich K.B., Varfolomeyev S.D.
- Журнал: Biochimica et Biophysica Acta - General Subjects
- Том: 1725
- Номер: 3
- Год издания: 2005
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 370
- Последняя страница: 376
- DOI: 10.1016/j.bbagen.2005.07.007
- Аннотация: Kinetic parameters (kPg and KPg) were determined for activation of Glu-plasminogen (Glu-Pg) and Lys-plasminogen (Lys-Pg) type I (with N-linked carbohydratechain at Asn-289) and type II (with unsubstituted Asn-289) by plasmin–staphylokinase (Pm–STA) complex. The KPg values for Glu-Pg I and Lys-Pg I (17.1 and 11.2 μM, respectively) were higher than those for Glu-Pg II and Lys-Pg II (14.9 and 5.4 μM, respectively), while only minor differences in the kPg values were observed between plasminogens type I and type II. Soluble fibrin significantly increased the kPg/KPg values for activation of all four plasminogens due to a decrease in the KPg values but did not alter the kPg values. However, the activation of plasminogens type I was stimulated by fibrin lesser degree than that of plasminogens type II. These findings indicate that N-glycosylation of kringle 3 of plasminogen decreases the stability of Pm–STA–Pg ternary enzyme–substrate complex in solution as well as interferes with its formation and rearrangement on the fibrin surface.
- Добавил в систему: Мухаметова Лилия Инилевна