Characterization of Coal Liquefaction Catalysts Using 1-Methylnaphthalene as a Model Compound

1979 ◽  
Vol 18 (4) ◽  
pp. 625-630 ◽  
Author(s):  
J. F. Patzer ◽  
Robert J. Farrauto ◽  
Angelo A. Montagna
2012 ◽  
Vol 531 ◽  
pp. 145-148
Author(s):  
Zong Hua Wang ◽  
Yan Li Gao ◽  
Jian Fei Xia ◽  
Fei Fei Zhang ◽  
Yan Zhi Xia ◽  
...  

A glycyrrhizin decorated graphene hybrid materials (GL-G) was synthesized, which is a layer-to-layer sandwich construction. The results of characterization indicate that a photo induced electron transfer process or efficient energy transferring along the GL-G interface. Furthermore, the as-made hybrid material was used as a modifier of the glassy carbon electrode to construct a sensor (GL-G/GCE). Using p-nitrophenol as a model compound, the novel sensor demonstrated a highly enhanced electrochemical activity for it. The peak current of p-nitrophenol was significantly improved at the sensor.


1991 ◽  
Vol 70 (1) ◽  
pp. 68-75
Author(s):  
Kaoru MASUDA ◽  
Saburo SAWADA ◽  
Osamu OKUMA ◽  
Tetsuro MATSUMURA

1992 ◽  
Vol 262 (5) ◽  
pp. F837-F842 ◽  
Author(s):  
E. Imesch ◽  
M. Moosmayer ◽  
B. M. Anner

The presence of circulating inhibitors able to decrease the renal Na-K-adenosinetriphosphatase (ATPase) activity (natriuretic hormones) was postulated some 30 years ago. In the present work, the natriuretic inhibitor HgCl2 was selected as a model compound for the structural characterization of a possible natriuretic pathway for Na-K-ATPase modification. The structural effects of Na-K-ATPase inhibition by HgCl2 were assessed by trypsinolysis of the blocked enzyme in comparison with untreated preparations. The results show that inactivation of Na-K-ATPase by HgCl2 leads to the release of the alpha-subunit from the membrane preferentially in the E2 conformation but also in the E1 conformation. Apparently, HgCl2 weakens the membrane anchoring of the alpha-subunit, presumably by loosening the alpha-beta-subunit interaction. By this mechanism, the sensitivity of the Na-K-ATPase to extracellular drugs, hormones, and antibodies, as well as to intracellular proteases and other regulatory factors, could be altered.


2000 ◽  
Vol 346 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Amnon ALBECK ◽  
Sharon KLIPER

Erythro peptidyl epoxides are selective inactivators of cysteine proteases. The alkylation site, both on the enzyme papain and on the epoxide itself, was characterized. The inactivation of papain with the peptidyl epoxide erythro benzyloxycarbonyl-Phe-Ala-epoxide was followed by total hydrolysis by acid. Mass spectral analysis of the hydrolysate revealed, in addition to the expected amino acids, a unique signal of m/z 209 (MH+). Its high-resolution mass spectrum and daughter peak analysis correspond to the product of alkylation on cysteine and the expected fragmentation. A similar MS pattern was obtained for a synthetic model compound corresponding to the expected hydrolysis product. A 13C NMR analysis of papain inactivated by a specifically 13C-labelled peptidyl epoxide indicated that the alkylation of the enzyme's cysteine residue occurs on the primary carbon of the epoxide moiety.


1989 ◽  
Vol 62 (12) ◽  
pp. 3959-3962 ◽  
Author(s):  
Yoshiharu Yoneyama ◽  
Yu Akaki ◽  
Tsutomu Kato

Fuel ◽  
2019 ◽  
Vol 243 ◽  
pp. 478-484 ◽  
Author(s):  
Yiming Zhang ◽  
Xiefei Zhu ◽  
Liqiang Zhang ◽  
Xifeng Zhu

Sign in / Sign up

Export Citation Format

Share Document