Incorporating Amino Acid Esters into Catalysts for Hydrogen Oxidation: Steric and Electronic Effects and the Role of Water as a Base

2012 ◽  
Vol 31 (19) ◽  
pp. 6719-6731 ◽  
Author(s):  
Sheri Lense ◽  
Ming-Hsun Ho ◽  
Shentan Chen ◽  
Avijita Jain ◽  
Simone Raugei ◽  
...  
1957 ◽  
Vol 106 (2) ◽  
pp. 327-343 ◽  
Author(s):  
Oscar D. Ratnoff ◽  
Irwin H. Lepow

Studies on an esterase derived from partially purified preparations of the first component of complement are described. The esterase hydrolyzed certain synthetic amino acid esters, among which N-acetyl-L-tyrosine ethyl ester was most susceptible. This was hydrolyzed maximally between pH 7.5 and 8.2, and at 41°C. The esterase could not be identified with other previously described hydrolytic enzymes. An esterase with similar properties could also be eluted from antigen-antibody aggregates which had been treated with serum. Human serum contained a heat-labile inhibitor of the esterase which could not be identified with any of the known components of complement. The esterase was also inhibited by certain reducing agents. The experiments described support the early hypothesis that complement exerts its action enzymatically, but the physiological role of the esterase derived from preparations of complement is not yet clear.


Synfacts ◽  
2006 ◽  
Vol 2006 (12) ◽  
pp. 1253-1253
Author(s):  
Y. Hamada ◽  
K. Makino ◽  
M. Iwasaki

2021 ◽  
Vol 294 ◽  
pp. 198290
Author(s):  
Lidia A. Baltina ◽  
Mann-Jen Hour ◽  
Ya-Chi Liu ◽  
Young-Sheng Chang ◽  
Su-Hua Huang ◽  
...  

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