Adsorption of urease as part of a complex protein mixture onto soil and its implications for enzymatic activity

2021 ◽  
Vol 171 ◽  
pp. 108026
Author(s):  
Rayla Pinto Vilar ◽  
Kaoru Ikuma
2008 ◽  
Vol 7 (10) ◽  
pp. 4525-4537 ◽  
Author(s):  
Zhi-Bin Ning ◽  
Qing-Run Li ◽  
Jie Dai ◽  
Rong-Xia Li ◽  
Chia-Hui Shieh ◽  
...  

2014 ◽  
Vol 42 (6) ◽  
pp. 1698-1703 ◽  
Author(s):  
Robert J. Beynon ◽  
Dean Hammond ◽  
Victoria Harman ◽  
Yvonne Woolerton

The increasing acceptance that proteins may exert multiple functions in the cell brings with it new analytical challenges that will have an impact on the field of proteomics. Many proteomics workflows begin by destroying information about the interactions between different proteins, and the reduction of a complex protein mixture to constituent peptides also scrambles information about the combinatorial potential of post-translational modifications. To bring the focus of proteomics on to the domain of protein moonlighting will require novel analytical and quantitative approaches.


2014 ◽  
Vol 86 (19) ◽  
pp. 9612-9619 ◽  
Author(s):  
Julien Breault-Turcot ◽  
Pierre Chaurand ◽  
Jean-Francois Masson

PROTEOMICS ◽  
2010 ◽  
Vol 10 (9) ◽  
pp. 1886-1890 ◽  
Author(s):  
Chris S. Hughes ◽  
Lynne M. Postovit ◽  
Gilles A. Lajoie

2012 ◽  
Vol 901 ◽  
pp. 34-40 ◽  
Author(s):  
Robert Ahrends ◽  
Björn Lichtner ◽  
Friedrich Buck ◽  
Diana Hildebrand ◽  
Marta Kotasinska ◽  
...  

BioResources ◽  
2007 ◽  
Vol 2 (1) ◽  
pp. 20-33
Author(s):  
Jung Myoung Lee ◽  
John A. Heitmann ◽  
Joel J. Pawlak

The effect of cellulase treatments on the rheology of carboxymethyl cellulose (CMC) solutions was studied using a rotational viscometer. The rheological behaviors of CMC solutions of different molecular mass and degrees of substitution where studied as a function of time after various treatments. These solutions were subjected to active and heat-denatured cellulase, a cationic polyelectrolyte (C-PAM), as well as different shear rates. A complex protein-polymer interaction was observed, leading to a potential error source in the measurement of enzymatic activity by changes in the intrinsic viscosity. The interaction was termed a polymeric effect and defined as a reduction in viscosity of the substrate solution without significant formation of reducing sugars from enzymatic hydrolysis. The cause of the reduction in viscosity appears to be related to the interaction between the enzymes as amphipathic particles and the soluble CMC. Thus, the polymeric effect may cause a considerable experimental error in the measurement of enzymatic activity by viscometric methods.


1959 ◽  
Vol 36 (2) ◽  
pp. 193-201 ◽  
Author(s):  
Julius A. Goldbarg ◽  
Esteban P. Pineda ◽  
Benjamin M. Banks ◽  
Alexander M. Rutenburg

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