Immunomorphological Changes in Neuronal and Non-Neuronal Structures in the Rat Intestine in a Toxin-Induced Model of Parkinsonism

Author(s):  
M. V. Ivanov ◽  
K. A. Kutukova ◽  
R. M. Khudoerkov ◽  
A. V. Stavrovskaya
Keyword(s):  
1977 ◽  
Vol 252 (13) ◽  
pp. 4501-4505 ◽  
Author(s):  
B E Kream ◽  
S Yamada ◽  
H K Schnoes ◽  
H F DeLuca

Surgery Today ◽  
2008 ◽  
Vol 38 (11) ◽  
pp. 1029-1035 ◽  
Author(s):  
Ahmet Guven ◽  
Turan Tunc ◽  
Turgut Topal ◽  
Mustafa Kul ◽  
Ahmet Korkmaz ◽  
...  

Amylase ◽  
2021 ◽  
Vol 5 (1) ◽  
pp. 13-22
Author(s):  
Gang Xiang ◽  
Piet L. Buwalda ◽  
Marc J.E.C van der Maarel ◽  
Hans Leemhuis

Abstract The 4,6-α-glucanotransferases of the glycoside hydrolase family 70 can convert starch into isomaltooligosaccharides (IMOs). However, no thermostable 4,6-α-glucanotransferases have been reported to date, limiting their applicability in the starch conversion industry. Here we report the identification and characterization of a thermostable 4,6-α-glucanotransferase from Bacillus coagulans DSM 1. The gene was cloned and the recombinant protein, called BcGtfC, was produced in Escherichia coli. BcGtfC is stable up to 66 °C in the presence of substrate. It converts debranched starch into an IMO product with a high percentage of α-1,6-glycosidic linkages and a relatively high molecular weight compared to commercially available IMOs. Importantly, the product is only partly and very slowly digested by rat intestine powder, suggesting that the IMO will provide a low glycaemic response in vivo when applied as food ingredient. Thus, BcGtfC is a thermostable 4,6-α-glucanotransferase suitable for the industrial production of slowly digestible IMOs from starch.


2008 ◽  
Vol 65 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Ganeshchandra Sonavane ◽  
Keishiro Tomoda ◽  
Akira Sano ◽  
Hiroyuki Ohshima ◽  
Hiroshi Terada ◽  
...  

1983 ◽  
Vol 24 (6) ◽  
pp. 746-752
Author(s):  
S E Schwartz ◽  
C Starr ◽  
S Bachman ◽  
P G Holtzapple

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