Design, synthesis, and characterization of chromogenic substrates of coagulation factor XIIIa.
Design, synthesis, and characterization of chromogenic substrates of coagulation factor XIIIa.
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凝血因子 XIIIa 显色底物的设计、合成和表征。
DOI：
10.1016/j.ab.2012.05.023
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发表时间：
2012
影响因子：
2.9
通讯作者：
T. Steinmetzer
中科院分区：
文献类型：
--
作者：
Kornelia Hardes;Gero L. Becker;M. Z. Hammamy;T. Steinmetzer
设计了一系列含Glu(PNA)的多肽，用于在405 nm处测定转谷氨酰胺酶因子XIIIA的活性。N末端第二位含有谷氨酸(PNA)残基的多肽具有最合适的底物性质。对于最好的底物12(H-酪氨酸-谷氨酸(PNA)-Val-Lys-Val-Ile-Gly-NH2)，Kcat/Km值为3531S−1M−1。尽管与先前报道的含有谷氨酰胺的天然底物如α2-抗纤溶酶和β-酪蛋白相比，谷氨酸(PNA)多肽的kcat/Km值降低了100多倍，但这些显色底物可以作为方便地测定FXIII-A2∗活性的有用工具，例如用于体外抑制剂筛选。以肽12为例，研究了不可逆抑制剂碘乙酸对FXIII-A2∗的抑制作用。
A series of Glu(pNA)-containing peptides was designed to determine the activity of the transglutaminase factor XIIIa at 405nm due to p-nitroaniline release. The most suitable substrate properties were found for peptides containing the Glu(pNA) residue in the second position from the N terminus. For the best substrate 12 (H-Tyr-Glu(pNA)-Val-Lys-Val-Ile-Gly-NH2), a kcat/Kmvalue of 3531s−1M−1was found. Although the kcat/Kmvalues of the Glu(pNA) peptides are more than 100-fold reduced compared with the previously reported cleavage of natural glutamine-containing substrates such as α2-antiplasmin and β-casein, these chromogenic substrates can be useful tools for convenient determination of FXIII-A2∗activity e.g., for in vitro inhibitor screening. As an example, peptide 12 was used to characterize the inhibition of FXIII-A2∗by the well-known irreversible inhibitor iodoacetic acid.
DOI：
10.1073/pnas.91.15.7296
发表时间：
1994-07-19
影响因子：
11.1
作者：
YEE, VC;PEDERSEN, LC;TELLER, DC
通讯作者：
TELLER, DC
用于激活纤维蛋白稳定因子（因子 XIIIa）和转谷氨酰胺酶的新型有色荧光胺底物。
影响因子：
2.9
作者：
Lorand,L;Parameswaran,KN;Velasco,PT;Hsu,LK;SiefringJr,GE
通讯作者：
SiefringJr,GE