Kinetic Study of Lipoxygenase-13-l-hydroperoxylinoleic Acid Interaction

1979 ◽  
Vol 43 (1) ◽  
pp. 167-169
Author(s):  
Hitoshi Aoshima ◽  
Tadahiko Kajiwara ◽  
Akikazu Hatanaka ◽  
Hiroshi Nakatani
Keyword(s):  
Kinetic Study ◽  
Acid Interaction ◽  
Hydroperoxylinoleic Acid

scholarly journals Kinetic study of lipoxygenase-13-L-hydroperoxylinoleic acid interaction.

1979 ◽  
Vol 43 (1) ◽  
pp. 167-169 ◽  
Author(s):  
Hitoshi AOSHIMA ◽  
Tadahiko KAJIWARA ◽  
Akikazu HATANAKA ◽  
Hiroshi NAKATANI
Keyword(s):  
Kinetic Study ◽  
Acid Interaction ◽  
Hydroperoxylinoleic Acid

Kinetic study of lipoxygenase-hydroperoxylinoleic acid interaction

1977 ◽  
Vol 486 (1) ◽  
pp. 121-126 ◽  
Author(s):  
Aoshima Hitoshi ◽  
Kajiwara Tadahiko ◽  
Hatanaka Akikazu ◽  
Nakatani Hiroshi ◽  
Hiromi Keitaro
Keyword(s):  
Kinetic Study ◽  
Acid Interaction ◽  
Hydroperoxylinoleic Acid

Biosynthesis of Leaf Alcohol: Kinetic Study of Lipoxygenase Activation Process Caused by Hydroperoxylinoleic Acid

1975 ◽  
Vol 39 (11) ◽  
pp. 2255-2257
Author(s):  
Hitoshi Aoshima ◽  
Tadahiko Kajiwara ◽  
Akikazu Hatanaka ◽  
Hiroshi Nakatani ◽  
Keitaro Hiromi
Keyword(s):  
Kinetic Study ◽  
Activation Process ◽  
Hydroperoxylinoleic Acid

scholarly journals Biosynthesis of leaf alcohol: Kinetic study of lipoxygenase activation process caused by hydroperoxylinoleic acid.

1975 ◽  
Vol 39 (11) ◽  
pp. 2255-2257 ◽  
Author(s):  
Hitoshi AOSHIMA ◽  
Tadahiko KAJIWARA ◽  
Akikazu HATANAKA ◽  
Hiroshi NAKATANI ◽  
Keitaro HIROMI
Keyword(s):  
Kinetic Study ◽  
Activation Process ◽  
Hydroperoxylinoleic Acid

A kinetic study of controlling nitrogen in process for boron steel by using30N2isotope gas

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):  
Kinetic Study ◽  
Boron Steel

Kinetic Study of the Effect of Heparin on the Amidase Activity of Trypsin, Plasmin and Urokinase

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev
Keyword(s):  
Kinetic Study ◽  
Active Center ◽  
Simultaneous Presence ◽  
Amidase Activity ◽  
Competitive Inhibitors ◽  
Uncompetitive Inhibitor

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.

A kinetic study of the metathesis of propene on a rhenium-aluminium catalyst

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