scholarly journals A high-throughput method for orthophosphate determination of thermostable membrane-bound pyrophosphatase activity

2018 ◽  
Vol 10 (6) ◽  
pp. 646-651 ◽  
Author(s):  
Keni Vidilaseris ◽  
Juho Kellosalo ◽  
Adrian Goldman

Membrane-bound pyrophosphatases (mPPases) are homodimeric integral membrane proteins that hydrolyse pyrophosphate into orthophosphates coupled to the active transport of protons or sodium ions across membranes.

Author(s):  
Louise Jank ◽  
Magda Targa Martins ◽  
Juliana Bazzan Arsand ◽  
Rodrigo Barcellos Hoff ◽  
Fabiano Barreto ◽  
...  

2007 ◽  
Vol 852 (1-2) ◽  
pp. 15-21 ◽  
Author(s):  
Fernando Goñi ◽  
Raul López ◽  
Arsenio Etxeandia ◽  
Esmeralda Millán ◽  
Pilar Amiano

FEBS Letters ◽  
1992 ◽  
Vol 296 (2) ◽  
pp. 158-162 ◽  
Author(s):  
Roberta Bianchi ◽  
Ileana Giambanco ◽  
Paolo Ceccarelli ◽  
Grazia Pula ◽  
Rosario Donato

2014 ◽  
Vol 70 (9) ◽  
pp. 2367-2375 ◽  
Author(s):  
Jobie Kirkwood ◽  
Julie Wilson ◽  
Simon O'Keefe ◽  
David Hargreaves

The crystallization of proteins is dependent on the careful control of numerous parameters, one of these being pH. The pH of crystallization is generally reported as that of the buffer; however, the true pH has been found to be as many as four pH units away. Measurement of pH with a meter is time-consuming and requires the reformatting of the crystallization solution. To overcome this, a high-throughput method for pH determination of buffered solutions has been developed with results comparable to those of a pH meter.


2011 ◽  
Vol 3 (11) ◽  
pp. 2557 ◽  
Author(s):  
Yun-Kai Lv ◽  
Yue-Na Sun ◽  
Li-Min Wang ◽  
Cui-Ling Jia ◽  
Han-Wen Sun

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