Effects of titanium dispersion state on distribution and reactivity of active centers in propylene polymerization with MgCl 2 ‐supported Ziegler‐Natta catalysts: A kinetic study based on active center counting

ChemCatChem ◽  
2020 ◽  
Vol 12 (20) ◽  
pp. 5140-5148
Author(s):  
Baiyu Jiang ◽  
Biao Zhang ◽  
Yintian Guo ◽  
Amjad Ali ◽  
Wenqi Guo ◽  
...  
RSC Advances ◽  
2016 ◽  
Vol 6 (79) ◽  
pp. 75023-75031 ◽  
Author(s):  
Qian Zhou ◽  
Ailian Wang ◽  
Huayi Li ◽  
Zhi Luo ◽  
Tao Zheng ◽  
...  

The volume of ecofriendly salicylate internal donors for propylene polymerization has an important impact on the catalyst active centers and microstructure of polypropylene.


2008 ◽  
Vol 287 (1-2) ◽  
pp. 45-52 ◽  
Author(s):  
Yury V. Kissin ◽  
Xinsheng Liu ◽  
David J. Pollick ◽  
Nancy L. Brungard ◽  
Main Chang

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.


2020 ◽  
Vol 62 (1) ◽  
pp. 14-21 ◽  
Author(s):  
V. V. Sukulova ◽  
A. A. Barabanov ◽  
T. B. Mikenas ◽  
M. A. Matsko ◽  
V. A. Zakharov

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