scholarly journals Detection of active proteasome structures in brain extracts: proteasome features of August rat brain with violations in monoamine metabolism

Oncotarget ◽  
2017 ◽  
Vol 8 (41) ◽  
pp. 70941-70957 ◽  
Author(s):  
Pavel A. Erokhov ◽  
Yulia V. Lyupina ◽  
Alexandra S. Radchenko ◽  
Anna A. Kolacheva ◽  
Yulia O. Nikishina ◽  
...  
Biochimie ◽  
1984 ◽  
Vol 66 (7-8) ◽  
pp. 531-537 ◽  
Author(s):  
Nicole Levilliers ◽  
Monique Peron-Renner ◽  
Gérard Coffe ◽  
Julio Pudles
Keyword(s):  

1970 ◽  
Vol 48 (10) ◽  
pp. 709-722 ◽  
Author(s):  
E. A. Hosein ◽  
A. Kato ◽  
E. Vine ◽  
A. M. Hill

Acetyl-l-carnitylcholine (l-ACCh) was identified in rat brain extracts on paper chromatograms developed in butanol–water for 138 h. l-ACCh was also identified in brain extracts fractionated on t.l.c. plates and on Sephadex G-10 columns. In every instance l-ACCh was separated from the acetylcholine (ACh) present and the ACh-like activity of l-ACCh was about 20% of the total activity in the extract. Both l-ACCh and ACh were found to be inseparable in a variety of chromatographic systems including electrophoresis. Treatment of these choline esters with cholinesterases showed that while true acetylcholinesterase hydrolyzed both l-ACCh and ACh, pseudocholinesterase destroyed only ACh. On a molar basis, the ACh-like activity of ACCh is one-half that of ACh on both the guinea pig ileum and frog rectus preparations. Like ACh, the ratio of the nicotinic to muscarinic potency of l-ACCh is unity. Mixtures of l-ACCh and ACh show summation of ACh-like activity on both the guinea pig ileum and frog rectus preparations.


1996 ◽  
Vol 39 ◽  
pp. 232-232
Author(s):  
Wako Nakajima ◽  
Akira Ishida ◽  
Hirokazu Arai ◽  
Yasushi Takahashi ◽  
Tadahiko Ito ◽  
...  

1976 ◽  
Vol 4 (1) ◽  
pp. 22-26 ◽  
Author(s):  
H. F. WOODS ◽  
A. R. GREEN ◽  
M. B. H. YOUDIM ◽  
D. G. GRAHAME-SMITH

1985 ◽  
Vol 63 (1) ◽  
pp. 1-12 ◽  
Author(s):  
W. Kehr ◽  
Gerlinde Debus ◽  
Ruth Neumeister

1993 ◽  
Vol 22 (6) ◽  
pp. 589-598 ◽  
Author(s):  
Erna B.H.W. Erdtsieck-Ernste ◽  
Matthijs G.P. Feenstra ◽  
Margriet H.A. Botterblom ◽  
Gerard J. Boer

1979 ◽  
Vol 29 (1) ◽  
pp. 54-65 ◽  
Author(s):  
John Y.-L. Yu ◽  
Hideo Namiki ◽  
Aubrey Gorbman

Peptides ◽  
1983 ◽  
Vol 4 (4) ◽  
pp. 585-587 ◽  
Author(s):  
J.A. Court ◽  
A.I. Smith ◽  
J.R. McDermott ◽  
J.A. Biggins ◽  
J.A. Edwardson

1980 ◽  
Vol 59 (s6) ◽  
pp. 45s-47s ◽  
Author(s):  
V. J. Dzau ◽  
Amy Brenner ◽  
Neremiah Emmett ◽  
E. Haber

1. The major angiotensin I-generating activity of rat brain extracts has a pH optimum different from that of renal renin and is not inhibited by renin specific antibody. 2. Affinity chromatography utilizing renin specific antibody, pepstatin and α-casein yielded fractions that resembled renal renin more closely with respect to antibody inhibition and pH optimum as well as an absence of the ability to hydrolyse haemoglobin. 3. We conclude that rat brain contains a host of enzymes with angiotensin I-generating activity including acid and neutral proteases and an enzyme with the immunochemical identity of renal renin. The biosynthetic origins of this renin-like protein remain uncertain.


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