scholarly journals Kinetic study of transverse electron-scale interface instability in relativistic shear flows

2020 ◽  
Vol 5 (5) ◽  
pp. 054403
Author(s):  
Peilin Yao ◽  
Hongbo Cai ◽  
Xinxin Yan ◽  
Wenshuai Zhang ◽  
Bao Du ◽  
...  
2015 ◽  
Vol 92 (2) ◽  
Author(s):  
E. P. Alves ◽  
T. Grismayer ◽  
R. A. Fonseca ◽  
L. O. Silva

2008 ◽  
Vol 105 (12) ◽  
pp. 601-608
Author(s):  
Seung Min Han ◽  
Dong Joon Min ◽  
Joo Hyun Park ◽  
Jung Ho Park ◽  
Jong Min Park
Keyword(s):  

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.


1981 ◽  
Vol 31 (1) ◽  
pp. 388-394 ◽  
Author(s):  
Mahmoud El-Sawi ◽  
Antonio Iannibello ◽  
Fernando Morelli ◽  
Ganfranco Gatalano ◽  
Francesco Intrieri ◽  
...  
Keyword(s):  

2011 ◽  
Vol 3 (5) ◽  
pp. 585-588
Author(s):  
B Dharma Rao B Dharma Rao ◽  
◽  
M Sridevi M Sridevi ◽  
P Vani P Vani

Sign in / Sign up

Export Citation Format

Share Document