FACTOR-XIII-MEDIATED CROSS-LINKING OF NH2-TERMINAL PEPTIDE OF ALPHA-2-PLASMIN INHIBITOR TO FIBRIN
FACTOR-XIII-MEDIATED CROSS-LINKING OF NH2-TERMINAL PEPTIDE OF ALPHA-2-PLASMIN INHIBITOR TO FIBRIN
复制标题
DOI：
10.1016/0014-5793(83)80645-0
复制
发表时间：
1983-01-01
期刊：
影响因子：
3.5
通讯作者：
AOKI, N
中科院分区：
文献类型：
--
作者：
ICHINOSE, A;TAMAKI, T;AOKI, N
α2‐纤溶酶抑制剂asn - gln - gln - gln - val - ser - pr - leu - thr - gly - leu - lys - NH2·AcOH的NH2‐末端12‐残基肽被发现是血浆转谷氨酰胺酶（活化凝血因子XIII）的良好底物，并被酶迅速结合到纤维蛋白中。高浓度的肽抑制了酶介导的α2 -纤溶蛋白抑制剂与纤维蛋白的交联，可能是通过与抑制剂竞争纤维蛋白α链的同一位点。
The NH2‐terminal 12‐residue peptide of α2‐plasmin inhibitor, Asn—Gln—Glu—Gln—Val—Ser—Pro—Leu—Thr—Gly—Leu—Lys—NH2·AcOH, was found to be a good substrate for plasma transglutaminase (activated blood coagulation factor XIII) and rapidly incorporated into fibrin by the enzyme. A high concentration of the peptide inhibited the enzyme‐mediated cross‐linking of α2‐plasmin inhibitor to fibrin probably by competing with the inhibitor for the same site of fibrin α‐chain.