Functional studies of streptokinase action on human plasminogen = 인체 플라스미노젠에 대한 스트렙토키나아제 작용의 기능적 연구

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Fibrinolysis is performed by the serum protease plasmin (plm), which is normally present in the blood as a precursor, plasminogen (plg). The plg is activated to plm by the plg activators, such as tissue-type plasminogen activator (t-PA) or urokinase-type plasminogen activator (u-PA). Streptokinase (SK), an extracellular protein produced by several strains of (-hemolytic streptococci, also activates plg to plm. SK is currently used as a therapeutic agent in treatment of the thromboembolic blockage, such as myocardial infarction. For the therapeutic use and the functional studies, a high-level expression plasmid for SK, pSK100, has been constructed. It contains a tac promoter, an ompA signal sequence, a SK structural gene (skc) and a rrnBT1T2 transcription terminator. E. coli JM109 carrying pSK100 produced about 5,000IU of SK per 1 ml of LB-ampicillin media. About 95% of the expressed SK were secreted into the periplasmic and extracellular fractions. The recombinant SK in high yield and purity may be a potential alternative source for the therapeutic agent. Because of its peculiar mechanism for plg activation, many researchers have long investigated SK. Unlike most of the plg activators, SK does not have proteolytic activity. It activates plg by the formation of an equimolar complex with plg. The SK-plg complex is an efficient proteolytic activator of plg. However, there are little reports on exact region of SK involved in activator complex formation with plg. In order to elucidate the interaction site or domain of SK with plg, C-terminal truncation analysis of SK was performed by exonuclease III method and PCR method. SK mutants, which lose 26, 33, 37, 40, 41, 46, 47, 50, 70, 97 or 124 amino acid residues from the C-terminus, were constructed. The truncated SKs were expressed in E.coli and purified. The 41 residue deletion (SKP373) from the C-terminus had not effect on the plg activation activity. However, the deletion of 46 amino acid residues (SKP368) resulted...
Advisors
Byun, Si-Myung변시명
Description
한국과학기술원 : 생물과학과,
Publisher
한국과학기술원
Issue Date
1998
Identifier
135086/325007 / 000935075
Language
eng
Description

학위논문(박사) - 한국과학기술원 : 생물과학과, 1998.2, [ ix, 113 p. ]

Keywords

Blood; SK; Plasminogen; Expression; 유전자발현; 혈액; 스트렙토키나아제; 플라스미노젠

URI
http://hdl.handle.net/10203/27423
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=135086&flag=dissertation
Appears in Collection
BS-Theses_Ph.D.(박사논문)
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