Human Hepatic ß-Glucuronidase: An Enzyme Kinetic Study

Enzyme ◽  
1985 ◽  
Vol 33 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Yen-Ching Ho ◽  
Le-Hong C. Ho ◽  
Kang-Jey Ho
Keyword(s):  
Kinetic Study ◽  
Enzyme Kinetic ◽  
Enzyme Kinetic Study

CYP2C9 Ile359 and Leu359 variants: enzyme kinetic study with seven substrates

2000 ◽  
Vol 10 (2) ◽  
pp. 95-104 ◽  
Author(s):  
Kenji Takanashi ◽  
Hitoshi Tainaka ◽  
Kaoru Kobayashi ◽  
Toshio Yasumori ◽  
Masakiyo Hosakawa ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Enzyme Kinetic ◽  
Enzyme Kinetic Study

scholarly journals New Fluorene Derivatives from Dendrobium gibsonii and Their α-Glucosidase Inhibitory Activity

Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 4931
Author(s):  
May Thazin Thant ◽  
Nutputsorn Chatsumpun ◽  
Wanwimon Mekboonsonglarp ◽  
Boonchoo Sritularak ◽  
Kittisak Likhitwitayawuid
Keyword(s):  
Kinetic Study ◽  
Inhibitory Activity ◽  
Spectroscopic Data ◽  
Enzyme Kinetic ◽  
Whole Plant ◽  
Noncompetitive Inhibitor ◽  
Inhibitory Activities ◽  
New Compounds ◽  
Enzyme Kinetic Study

Two new compounds, dihydrodengibsinin (1) and dendrogibsol (2), were isolated from the whole plant of Dendrobium gibsonii, together with seven known compounds (3–9). The structures of the new compounds were elucidated by their spectroscopic data. All these isolates were evaluated for their α-glucosidase inhibitory activities. Dendrogibsol (2) and lusianthridin (7) showed strong α-glucosidase inhibitory activity when compared with acarbose. An enzyme kinetic study revealed that dendrogibsol (2) is a noncompetitive inhibitor of α-glucosidase.

Isolation and identification of α-glucosidase inhibitory constituents from the seeds of Vigna nakashimae: Enzyme kinetic study with active phytochemical

2018 ◽  
Vol 266 ◽  
pp. 483-489 ◽  
Author(s):  
Tae Joung Ha ◽  
Seok Bo Song ◽  
Jeeyeon Ko ◽  
Chang-Hwan Park ◽  
Jong-Min Ko ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Enzyme Kinetic ◽  
Isolation And Identification ◽  
Enzyme Kinetic Study

Enzyme kinetic study of a new cardioprotective agent, KR-32570 using human liver microsomes and recombinant CYP isoforms

2007 ◽  
Vol 30 (4) ◽  
pp. 469-474 ◽  
Author(s):  
Hyojin Kim ◽  
Kyung-Ah Seo ◽  
Hyunmi Kim ◽  
Hye Suk Lee ◽  
Choong-Hwan Lee ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
Enzyme Kinetic ◽  
Cyp Isoforms ◽  
Enzyme Kinetic Study

scholarly journals Enzyme Kinetic Study for Degradation of Phytic acid by Phytase

KSBB Journal ◽  
2011 ◽  
Vol 26 (4) ◽  
pp. 300-304
Author(s):  
Jae-Seok Kim ◽  
Jae-Heung Lee
Keyword(s):  
Kinetic Study ◽  
Phytic Acid ◽  
Enzyme Kinetic ◽  
Enzyme Kinetic Study

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.

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