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

ChemInform ◽  
2010 ◽  
Vol 29 (51) ◽  
pp. no-no
Author(s):  
A. V. RUKAVISHNIKOV ◽  
M. P. SMITH ◽  
G. B. BIRRELL ◽  
J. F. W. KEANA ◽  
O. H. GRIFFITH
Keyword(s):  
Phospholipase C ◽  
Fluorogenic Substrate

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

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

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.

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

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

1998 ◽  
Vol 39 (37) ◽  
pp. 6637-6640 ◽  
Author(s):  
Aleksey V. rukavishnikov ◽  
Miles P. Smith ◽  
G. Bruce Birrell ◽  
John F.W. Keana ◽  
O. Hayes Griffith
Keyword(s):  
Phospholipase C ◽  
Fluorogenic Substrate
Sign in / Sign up

Export Citation Format

Share Document