New Polymeric Supports Can Improve Enzymatic Catalysis in Non-Conventional Media

2002 ◽  
Vol 230-232 ◽  
pp. 475-478 ◽  
Author(s):  
J.M.S. Rocha ◽  
M. Helena Gil ◽  
F.A.P. Garcia
Author(s):  
А.С. Шадрина ◽  
И.В. Терешкина ◽  
Я.З. Плиева ◽  
Д.Н. Кушлинский ◽  
Д.О. Уткин ◽  
...  

Матриксные металлопротеиназы (ММП) - ферменты класса гидролаз, осуществляющие ферментативный катализ с помощью связанного в активном центре иона цинка. Функции ММП разнообразны, и нарушение баланса их активности может быть одним из этиологических факторов различных заболеваний. В данном обзоре рассмотрена классификация ММП человека, особенности их структуры и регуляции, а также роль в физиологических и патологических процессах в организме человека. Приведен перечень наиболее изученных на настоящий момент полиморфных вариантов генов MMП, описаны их функциональные эффекты и представлены результаты ассоциативных исследований. Matrix metalloproteinases (MMPs) are enzymes of the hydrolase class that carry out enzymatic catalysis with the help of a zinc ion bound in the active center. MMP functions are diverse, and a disturbance in the balance of their activity may be one of the etiological factors of various diseases. In this review, the classification of human MMP, the features of their structure and regulation, as well as the role in physiological and pathological processes in the human body are considered. A list of the most studied polymorphic versions of MMP genes has been given, their functional effects have been described, and the results of associative studies have been presented.


Author(s):  
Paulo F.A. Costa ◽  
Rafael de Abreu ◽  
Andressa B. Fontana ◽  
Haidi D. Fiedler ◽  
Anthony J. Kirby ◽  
...  

Biochemistry ◽  
2021 ◽  
Author(s):  
Pedro Ojeda-May ◽  
Ameeq UI Mushtaq ◽  
Per Rogne ◽  
Apoorv Verma ◽  
Victor Ovchinnikov ◽  
...  

2001 ◽  
Vol 73 (12) ◽  
pp. 1993-1999 ◽  
Author(s):  
P. V. Climent ◽  
M. L. M. Serralheiro ◽  
M. J. F. Rebelo

An amperometric biosensor based on the enzyme polyphenoloxidase (PPO), which makes the bioelectrocatalysis of phenolic compounds, was developed and optimized using cathecol as substrate. Polyethersulphone membranes were used for enzyme immobilization. Polyphenoloxidase oxidizes monophenols (cresolase activity) and diphenols (catecholase activity) into the corresponding o-quinones; the o-quinones formed in the enzymatic catalysis are then reduced back to cathecol at ­200 mV (vs. Ag, AgCl) at a platinum electrode. The polyphenoloxidase immobilized was from commercial origin or extracted from mushrooms. p-Cresol and phenol substrates were also tested. Reproducibility, response time, linearity, sensitivity, and stability of the biosensor were studied.


ChemInform ◽  
2006 ◽  
Vol 37 (43) ◽  
Author(s):  
Bart M. L. Dioos ◽  
Ivo F. J. Vankelecom ◽  
Pierre A. Jacobs
Keyword(s):  

1994 ◽  
Vol 8 (6) ◽  
pp. 635-650 ◽  
Author(s):  
George D. Vaughn ◽  
Bruce G. Frushour ◽  
William C. Dale

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Shuiqin Jiang ◽  
Lujia Zhang ◽  
Dongbin Cui ◽  
Zhiqiang Yao ◽  
Bei Gao ◽  
...  

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