Evaluation of Some Fluorogenic Substrates for Continuous Assay of Aminopeptidase P

1997 ◽  
Vol 253 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Susan J. Hawthorne ◽  
Patrick Harriott ◽  
Jaeseung Lim ◽  
Anthony J. Turner ◽  
Brian Walker ◽  
...  
1982 ◽  
Vol 125 (3) ◽  
pp. 609-615 ◽  
Author(s):  
Gideon FLEMINGER ◽  
Amos CARMEL ◽  
Dalia GOLDENBERG ◽  
Arieh YARON

FEBS Letters ◽  
1988 ◽  
Vol 227 (2) ◽  
pp. 171-174 ◽  
Author(s):  
Jürgen Lasch ◽  
Regine Koelsch ◽  
Torsten Steinmetzer ◽  
Ulf Neumann ◽  
Hans-Ulrich Demuth

2000 ◽  
Vol 283 (1) ◽  
pp. 39-48 ◽  
Author(s):  
Kimito Washiya ◽  
Tetsuya Furuike ◽  
Fumio Nakajima ◽  
Yuan C. Lee ◽  
Shin-Ichiro Nishimura

2001 ◽  
Vol 12 (2) ◽  
pp. 307-313 ◽  
Author(s):  
Tatiana O. Zaikova ◽  
Aleksey V. Rukavishnikov ◽  
G. Bruce Birrell ◽  
O. Hayes Griffith ◽  
John F. W. Keana

1997 ◽  
Vol 78 (04) ◽  
pp. 1193-1201 ◽  
Author(s):  
Saulius Butenas ◽  
Maria E DiLorenzo ◽  
Kenneth G Mann

SummarySelective, sensitive assays for the quantitation of serine proteases involved in coagulation and fibrinolysis have been developed employing fluorogenic substrates containing a 6-amino-1-naphthalenesulfonamide leaving group (PNS-substrates). Over one hundred substrates were evaluated for hydrolysis by the serine proteases of blood coagulation and fibrinolysis, and substrate structure-efficiency correlations were examined. PNS-substrates which contain Lys in the P1 position are specific for Lys-plasmin and are either not hydrolyzed or hydrolyzed at a relatively low rate by factor Xa, thrombin, or urokinase-type plasminogen activator (uPA). These substrates allow quantitation of Lys-plasmin at concentrations as low as 1 pM. Eighteen of over 90 substrates tested for factor XIa are hydrolyzed by this enzyme at a relatively high rate reaching a kcat value of 170 s-1 and allowing quantitation of factor XIa at 10 fM. Eighteen of almost 90 PNS-substrates tested display high specificity for thrombin, some exceeding that for factor Xa by > 10,000-fold and > 100-fold for activated protein C (APC). Seven of these substrates have a over 100 s-1 and three of them have a KM below 1 μM. They allow the quantitation of thrombin at concentrations as low as 20 fM. For APC, uPA and the factor Vila/tissue factor complex, quantitation is feasible at 1 pM concentration. For factor Xa and factor VIIa the limits are 0.4 pM and 40 pM respectively. The PNS-substrates presented in this study may be employed for the development of direct and sensitive serine protease assays.


2017 ◽  
Vol 14 (3) ◽  
pp. 330-338
Author(s):  
Polaboina Snigdha ◽  
Pachineella Rao ◽  
Nagu Prabhu ◽  
Insaf Qureshi

2021 ◽  
Author(s):  
Xueyan Huang ◽  
Qian Lei ◽  
Shuai Huang ◽  
Hongliang Zeng ◽  
Bin Feng ◽  
...  

We reported a rational strategy to deliberately construct the first asymmetric tetraarylimidazole-based AIE probe, integrating AIE behavior in synergy with ESIPT character to ratiometric imaging of endogenous LAP for the...


1981 ◽  
Vol 110 (1) ◽  
pp. 232-239 ◽  
Author(s):  
Kazuo Murakami ◽  
Tamiko Ohsawa ◽  
Shigehisa Hirose ◽  
Katsumi Takada ◽  
Shumpei Sakakibara

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