Kinetic Analysis of Oxygen Utilization during Cofactor Biogenesis in a Copper-Containing Amine Oxidase from Yeast†

Biochemistry ◽  
2000 ◽  
Vol 39 (13) ◽  
pp. 3699-3707 ◽  
Author(s):  
Benjamin Schwartz ◽  
Joanne E. Dove ◽  
Judith P. Klinman
2002 ◽  
Vol 58 (s1) ◽  
pp. c298-c298
Author(s):  
M. Kim ◽  
T. Okajima ◽  
S. Kishishita ◽  
M. Yoshimura ◽  
A. Kawamori ◽  
...  

2007 ◽  
Vol 129 (37) ◽  
pp. 11524-11534 ◽  
Author(s):  
Robyn H. Moore ◽  
M. Ashley Spies ◽  
Matthew B. Culpepper ◽  
Takeshi Murakawa ◽  
Shun Hirota ◽  
...  

Author(s):  
Misa Kim ◽  
Toshihide Okajima ◽  
Seiichiro Kishishita ◽  
Megumi Yoshimura ◽  
Asako Kawamori ◽  
...  

Biochemistry ◽  
2005 ◽  
Vol 44 (36) ◽  
pp. 12041-12048 ◽  
Author(s):  
Toshihide Okajima ◽  
Sei'ichiro Kishishita ◽  
Yen-Chen Chiu ◽  
Takeshi Murakawa ◽  
Misa Kim ◽  
...  

Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.


1965 ◽  
Vol 13 (01) ◽  
pp. 155-175 ◽  
Author(s):  
H. C Hemker ◽  
P.W Hemker ◽  
E. A Loeliger

SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.


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