Synthesis of Fluorogenic Substrates for Continuous Assay of Phosphatidylinositol-Specific Phospholipase C

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
Keyword(s):  
Phospholipase C ◽  
Fluorogenic Substrates ◽  
Continuous Assay

A CHROMOGENIC SUBSTRATE FOR THE CONTINUOUS ASSAY OF MAMMALIAN PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C

1997 ◽  
Vol 7 (10) ◽  
pp. 1239-1242 ◽  
Author(s):  
Aleksey V Rukavishnikov ◽  
Margret Ryan ◽  
O.Hayes Griffith ◽  
John F.W Keana
Keyword(s):  
Phospholipase C ◽  
Chromogenic Substrate ◽  
Continuous Assay

scholarly journals Allosteric Interactions within Subsites of a Monomeric Enzyme: Kinetics of Fluorogenic Substrates of PI-Specific Phospholipase C

2003 ◽  
Vol 84 (5) ◽  
pp. 3264-3275 ◽  
Author(s):  
G. Bruce Birrell ◽  
Tatiana O. Zaikova ◽  
Aleksey V. Rukavishnikov ◽  
John F.W. Keana ◽  
O. Hayes Griffith
Keyword(s):  
Enzyme Kinetics ◽  
Phospholipase C ◽  
Fluorogenic Substrates ◽  
Allosteric Interactions ◽  
Kinetics Of

ChemInform Abstract: Synthesis of a New Fluorogenic Substrate for the Continuous Assay of Mammalian Phosphoinositide-Specific Phospholipase C.

ChemInform ◽  
2010 ◽  
Vol 30 (33) ◽  
pp. no-no
Author(s):  
Aleksey V. Rukavishnikov ◽  
Tatiana O. Zaikova ◽  
G. Bruce Birrell ◽  
John F. W. Keana ◽  
O. Hyes Griffith
Keyword(s):  
Phospholipase C ◽  
Fluorogenic Substrate ◽  
Continuous Assay

Synthesis of a new fluorogenic substrate for the continuous assay of mammalian phosphoinositide-specific phospholipase C

1999 ◽  
Vol 9 (8) ◽  
pp. 1133-1136 ◽  
Author(s):  
Aleksey V. Rukavishnikov ◽  
Tatiana O. Zaikova ◽  
G.Bruce Birrell ◽  
John F.W. Keana ◽  
O. Hayes Griffith
Keyword(s):  
Phospholipase C ◽  
Fluorogenic Substrate ◽  
Continuous Assay

ChemInform Abstract: A Chromogenic Substrate for the Continuous Assay of Mammalian Phosphoinositide-Specific Phospholipase C.

ChemInform ◽  
2010 ◽  
Vol 28 (39) ◽  
pp. no-no
Author(s):  
A. V. RUKAVISHNIKOV ◽  
M. RYAN ◽  
O. H. GRIFFITH ◽  
J. F. W. KEANA
Keyword(s):  
Phospholipase C ◽  
Chromogenic Substrate ◽  
Continuous Assay

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 ◽  
...  
Keyword(s):  
Fluorogenic Substrates ◽  
Aminopeptidase P ◽  
Continuous Assay

Design of Fluorogenic Substrates for Continuous Assay of Sialyltransferase by Resonance Energy Transfer

2000 ◽  
Vol 283 (1) ◽  
pp. 39-48 ◽  
Author(s):  
Kimito Washiya ◽  
Tetsuya Furuike ◽  
Fumio Nakajima ◽  
Yuan C. Lee ◽  
Shin-Ichiro Nishimura
Keyword(s):  
Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorogenic Substrates ◽  
Continuous Assay

scholarly journals Kinetic mechanism of Clostridium perfringens phospholipase C. Hydrolysis of a thiophosphate analogue of lysophosphatidylcholine

1991 ◽  
Vol 280 (2) ◽  
pp. 407-410 ◽  
Author(s):  
P R Young ◽  
W R Snyder ◽  
R F McMahon
Keyword(s):  
Phospholipase C ◽  
Clostridium Perfringens ◽  
Kinetic Mechanism ◽  
Compound I ◽  
Nitrobenzoic Acid ◽  
Competitive Mechanism ◽  
Simple Slope ◽  
Continuous Assay ◽  
Hydrolysis Of

The hydrolysis of S-[2-(hexadecanoyloxy)ethyl]thiophosphocholine (I), an analogue of lysophosphatidylcholine, by Clostridium perfringens phospholipase C, was followed at pH 7.5, 37 degrees C and I 1.0 (maintained with KCl), in a continuous assay, by monitoring the reduction of 5,5′-dithiobis-(2-nitrobenzoic acid) at 412 nm. Simple saturation kinetics are observed with linear mixed-type slope-intercept effects for the hydrolysis of compound (I) with variable [Ca2+] at fixed concentrations of compound (I) and a simple slope effect as [compound (I)] is varied at fixed concentrations of Ca2+. These data are consistent with a simple ordered rapid-equilibrium mechanism in which Ca2+ binds to the enzyme first followed by substrate. The observed kinetic constants at pH 7.5, 37 degrees C and I 1.0 are K1 = 12.0 mM (Ca2+ dissociation), K2 = 36 microM [compound (I) dissociation] and Vmax. = 552 microM.min-1.mg-1. Alkane diammonium salts inhibit the enzyme by a non-competitive mechanism that involves binding to free enzyme, E.Ca2+ and E.Ca2+.S. The use of the simple micellarized substrate under these conditions allows the determination of kinetic and inhibition constants without complications arising from enzyme-micelle interactions.

scholarly journals Synthesis and Evaluation of Fluorogenic Substrates for Phospholipase D and Phospholipase C

2006 ◽  
Vol 8 (12) ◽  
pp. 2575-2578 ◽  
Author(s):  
Tyler M. Rose ◽  
Glenn D. Prestwich
Keyword(s):  
Phospholipase C ◽  
Phospholipase D ◽  
Fluorogenic Substrates
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