Characterization of Polyethylene Glycolated Horseradish Peroxidase in Organic Solvents:  Generation and Stabilization of Transient Catalytic Intermediates at Low Temperature

1998 ◽  
Vol 120 (32) ◽  
pp. 8020-8025 ◽  
Author(s):  
Shin-ichi Ozaki ◽  
Yuji Inada ◽  
Yoshihito Watanabe
Catalysts ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 168 ◽  
Author(s):  
Ye Yuan ◽  
Jia Xu ◽  
Zhenyu Zhao ◽  
Hui Li ◽  
Kai Wang ◽  
...  

In this study, we reported on a novel mimetic peroxidase, deuterohemin–Ala–His–Glu, (Dh–A–H–E). The kinetic parameters of Dh–A–H–E suggested that it was a mimetic peroxidase and followed the ping–pong mechanism. Compared to horseradish peroxidase, Dh–A–H–E exhibited excellent stability when tested at different pH and temperatures, and using different organic solvents. Based on our above results, a new method using Dh–A–H–E has successfully been developed for the fast and quantitative detection of trace amounts of glucose.


2015 ◽  
Vol 135 (7) ◽  
pp. 733-738 ◽  
Author(s):  
Yasushi Kobayashi ◽  
Yoshihiro Nakata ◽  
Tomoji Nakamura ◽  
Mayumi B. Takeyama ◽  
Masaru Sato ◽  
...  
Keyword(s):  

1967 ◽  
Vol 15 (7) ◽  
pp. 375-380 ◽  
Author(s):  
WERNER STRAUS

Small phagosomes (micropinocytic vesicles and vacuoles) which had taken up injected horseradish peroxidase were identified by staining for peroxidase with benzidine and H2O2. Because of the small size of the granules and the possibility of artifacts, previously described procedures had to be modified in several respects. Prefixation of the tissue by perfusion at 37°C prevented artifacts of diffusion and adsorption of peroxidase. The blue product of the reaction of peroxidase with benzidine in the small phagosomes was preserved and fading to brown was prevented by cooling the tissue section to –10° to –15°C during its processing through polar media. The blue reaction product was stable as soon as the section was transferred to an apolar medium. Small phagosomes were visualized together with lysosomes and phago-lysosomes in the same cells by double staining for acid phosphatase and peroxidase in contrasting colors. The incubation for acid phosphatase was performed at 4°C since low temperature increased the stability of peroxidase in the acid medium. Factors which form the basis for other improvements of the procedure are discussed.


2017 ◽  
Vol 122 (8) ◽  
pp. 084103 ◽  
Author(s):  
E. Smirnova ◽  
A. Sotnikov ◽  
S. Ktitorov ◽  
H. Schmidt

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