Sequence of plasmin proteolysis at the NH2-terminus of the b beta-chain of human fibrinogen.
Sequence of plasmin proteolysis at the NH2-terminus of the b beta-chain of human fibrinogen.
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人纤维蛋白原 b β 链 NH2 末端的纤溶酶蛋白水解序列。
DOI：
10.1016/0003-2697(83)90116-1
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发表时间：
1983
影响因子：
2.9
通讯作者：
Canfield,RE
中科院分区：
文献类型：
--
作者：
Koehn,JA;Hurlet-Jensen,A;Nossel,HL;Canfield,RE
采用高效液相色谱法（HPLC），我们分离并定量了纤溶酶蛋白水解从人纤维蛋白原B β链NH 2-末端释放的肽。通过氨基酸组成和用于纤维蛋白肽B检测的放射免疫测定法鉴定肽。B β 1 - 42是纤溶酶有限水解过程中最早释放的片段。这种肽的水平达到最大值，然后在消化过程中开始下降。此外，B β 1 - 21和FP B水平的增加伴随着B β 1 - 42的产生。使用纯化的B β 1 - 42作为底物，显示优先裂解发生在21 - 22键处，在14 - 15键处有较小的裂解。极限消化产生两种主要组分，通过HPLC分离：B β 1 - 14（FP B）和β 22 - 42。在14 - 15键处的裂解速率，这是凝血酶蛋白水解的常规位点，不受水蛭素的添加的影响，表明这不是凝血酶的痕量污染的结果。我们还检测了多种纤维蛋白原衍生物的B β链的NH 2-末端区域的纤溶酶蛋白水解，并发现了类似的B β 1 - 42释放模式。利用HPLC数据，我们估计β 21 - 22键和β 14 - 15键的胞质裂解Km分别为1.8 × 10 − 5m和2.8 × 10 − 5m。在另一份报告（A。Hurlet-Jensen，J. A. Koehn和H. L.诺塞尔，血栓。Res.29，609 - 617（1983）），我们估计纤维蛋白原中β 42 - 43键的胞质裂解Km为7.0 × 10 − 7 m。总之，这些数据表明了一系列事件，其中B β 1 - 42最初在纤溶酶消化过程中从纤维蛋白原上裂解。一旦从其母体分子中释放，B β 1 - 42可优先在21 - 22键处经历进一步的纤溶酶攻击以产生B β 1 - 21和β 22 - 42。然后纤溶酶可以攻击B β 1 - 21的14 - 15键以释放FP B。这里提供的动力学数据表明，这些二级裂解可能是非常有限的体内。
Employing high-performance liquid chromatography (HPLC), we have isolated and quantified the peptides that are released from the NH2-terminus of human fibrinogen Bβ-chains by plasmin proteolysis. The peptides were identified by amino acid composition and by a radioimmunoassay developed for fibrinopeptide B detection. Bβ1–42 was the earliest fragment released during limited plasmin proteolysis. The level of this peptide reached a maximum and then began to decline during the course of the digestion. In addition, increasing levels of Bβ1–21 and of FPB followed the production of Bβ1–42. Using purified Bβ1–42 as a substrate, preferential cleavage was shown to occur at the 21–22 bond, with a minor cleavage at the 14–15 bond. Exhaustive digestion yielded two major components which were separated by HPLC: Bβ1–14 (FPB) and β22–42. The rate of cleavage at the 14–15 bond, which is the customary site of thrombin proteolysis, was not affected by the addition of hirudin indicating that this was not the result of trace contamination with thrombin. We have also examined plasmin proteolysis at the NH2-terminal region of the Bβ-chains of a variety of fibrinogen derivatives and have found similar patterns of Bβ1–42 release. Using HPLC data, we have estimated the Kmfor plasmic cleavage of the β21–22 bond to be 1.8 × 10−5m and of the β14–15 bond to be 2.8 × 10−5m. In another report (A. Hurlet-Jensen, J. A. Koehn, and H. L. Nossel, Thromb. Res.29, 609–617 (1983)), we estimated the Kmfor plasmic cleavage of the β42–43 bond in fibrinogen to be 7.0 × 10−7m. Taken together, these data indicate a sequence of events in which Bβ1–42 was initially cleaved from fibrinogen during plasmin digestion. Once released from its parent molecule, Bβ1–42 can undergo further plasmin attack preferentially at the 21–22 bond to yield Bβ1–21 and β22–42. Plasmin can then attack Bβ1–21 at the 14–15 bond to release FPB. The kinetic data presented here indicate that these secondary cleavages are likely to be very limited in vivo.
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