Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis.
Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis.
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从黄绿竹叶青毒液中分离出的凝血因子 IX/因子 X 结合蛋白的结合特性。
DOI：
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发表时间：
1994
期刊：
影响因子：
--
通讯作者：
T. Morita
中科院分区：
文献类型：
--
作者：
H. Atoda;N. Yoshida;M. Ishikawa;T. Morita
采用酶联免疫吸附法研究了从黄毒蛇毒中分离的凝血因子IX/因子x结合抗凝蛋白（IX/X-bp）的结合特性。在Ca2+浓度为0.4 mM和1 mM时，IX/X-bp分别与因子IX和因子X的半最大结合和最大结合。在1 mM Ca2+离子存在下，IX/X-bp与固相牛因子IX和固相牛因子X的半最大结合浓度分别为0.4 +/- 0.1 nM和1.1 +/- 0.4 nM。IX/X-bp与牛因子IXa和Xa以及人因子IX和X的结合动力学与牛因子IX和X的结合动力学相似。在本实验条件下，IX/X-bp不结合除IX/IXa和X/Xa因子以外的固相凝血因子，如凝血酶原、因子VII、蛋白C和蛋白Z。为了定位IX/X-bp在凝血因子上的结合位点，我们检测了IX/X-bp与因子IX和X衍生的各种片段的结合能力。IX/X-bp与固相因子IX的结合被液相中含有4-羧基谷氨酸（Gla）结构域的肽（残基1-42）所抑制，但未被无Gla结构域的因子IXa β’所抑制。IX/X-bp在9.2 +/- 1.9 nM处与因子IX固相Gla-domain肽结合达到半最大值。部分还原了因子X，制备了s -羧甲基化的因子X轻链和重链。IX/X-bp与s -羧甲基化因子X的轻链结合，但不与重链结合。IX/X-bp与固相因子X的结合受到因子X的gla结构域肽（残基1-44）的抑制，而不受无gla结构域因子X的抑制。重组人蛋白C，其gla结构域（残基1-43）已被人因子X的残基1-43取代，其结合亲和力约为完整人因子X的十分之一。IX/X-bp完全不能与人蛋白C结合。这些数据表明，IX/X-bp是在Ca2+离子存在下与因子IX和X的gla结构域结合的蛋白。
The binding properties of the coagulation factor IX/factor X-binding anticoagulant protein (IX/X-bp) isolated from the venom of Trimeresurus flavoviridis (habu snake) were investigated with an enzyme-linked immunosorbent assay. The half-maximal binding and maximal binding of IX/X-bp to both factors IX and X were observed at concentrations of Ca2+ ions of 0.4 mM and 1 mM, respectively. Concentration of IX/X-bp at half-maximal binding to solid-phase bovine factor IX and solid-phase bovine factor X were 0.4 +/- 0.1 nM and 1.1 +/- 0.4 nM, respectively, in the presence of 1 mM Ca2+ ions. The kinetics of binding activity of IX/X-bp to bovine factors IXa and Xa and to human factors IX and X resembled those of the binding to bovine factors IX and X. IX/X-bp did not bind to solid-phase coagulation factors other than factor IX/IXa and factor X/Xa, for example, prothrombin, factor VII, protein C, and protein Z, under the conditions of the experiment. To localize the binding sites of IX/X-bp on the coagulation factors, the ability of IX/X-bp to bind to various fragments derived from factors IX and X was examined. The binding of IX/X-bp to solid-phase factor IX was inhibited by a peptide containing the 4-carboxyglutamic acid (Gla) domain derived from factor IXa beta' (residues 1-42) in the liquid phase, but the binding was not inhibited by Gla-domainless factor IXa beta'. Half-maximal binding of IX/X-bp to solid-phase Gla-domain peptide of factor IX occurred at 9.2 +/- 1.9 nM. Factor X was partially reduced and the S-carboxymethylated light and heavy chains of factor X were prepared. IX/X-bp bound to the S-carboxymethylated light chain of factor X but not to the heavy chain. The binding of IX/X-bp to solid-phase factor X was inhibited by the Gla-domain peptide of factor X (residues 1-44) but not by Gla-domainless factor X. IX/X-bp bound to PCGFX, a recombinant human protein C whose Gla-domain region (residues 1-43) had been replaced by residues 1-43 of human factor X. The affinity of binding was about one tenth of that to intact human factor X. IX/X-bp was unable to bind at all to human protein C. These data indicate that IX/X-bp is a protein that binds to the Gla-domain regions of factors IX and X in the presence of Ca2+ ions.
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Ca2 与人因子 IX 协同结合。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Bajaj,SP
通讯作者：
Bajaj,SP
DOI：
--
发表时间：
1989-12
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
H. Nishimura;S. Kawabata;W. Kisiel;S. Hase;T. Ikenaka;T. Takao;Y. Shimonishi;S. Iwanaga
通讯作者：
H. Nishimura;S. Kawabata;W. Kisiel;S. Hase;T. Ikenaka;T. Takao;Y. Shimonishi;S. Iwanaga
影响因子：
56.9
作者：
WEIS, WI;KAHN, R;HENDRICKSON, WA
通讯作者：
HENDRICKSON, WA
与金属结合和酶原激活相关的牛 X 因子的结构转变。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Keyt,B;Furie,BC;Furie,B
通讯作者：
Furie,B
钙结合和酶原激活时人因子 IX 蛋白酶结构域中抗体探测的构象转变：蛋白酶结构域中推定的高亲和力 Ca(2 ) 结合位点。
DOI：
10.1073/pnas.89.1.152
发表时间：
1992
影响因子：
11.1
作者：
Bajaj,SP;Sabharwal,AK;Gorka,J;Birktoft,JJ
通讯作者：
Birktoft,JJ