Effect of adrenalectomy on enzyme activity in the mucous membrane of the rat small intestine

1974 ◽  
Vol 78 (5) ◽  
pp. 1281-1283
Author(s):  
K. Rakhimov ◽  
U. Z. Kadyrov ◽  
B. Zaripov
1973 ◽  
Vol 131 (2) ◽  
pp. 375-380 ◽  
Author(s):  
T. Noguchi ◽  
M. Nishino ◽  
R. Kido

Tryptophan 5-hydroxylase was partially purified from rat small intestine and characterized. The enzyme activity was mainly localized in the distal one-fourth of the small intestine. The enzyme required Fe2+, 2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine and oxygen for full activity. The pH optimum of the reaction was 8.0. The hydroxylation rate of d-tryptophan by the enzyme was one-third that of l-tryptophan. l-Phenylalanine and l-tyrosine could not serve as substrates. The physiological significance of the enzyme is discussed.


1987 ◽  
Vol 21 (4) ◽  
pp. 212A-212A
Author(s):  
Elizabeth L Engelhardt ◽  
James C Beggs ◽  
Josef Neu ◽  
Donald V Eitzman

1984 ◽  
Vol 64 (5) ◽  
pp. 136-137 ◽  
Author(s):  
D. S. PARKER ◽  
R. C. MACGREGOR ◽  
HEATHER J. FINLAYSON ◽  
P. STOCKILL ◽  
J. BALIOS

Inclusion of avoparcin in the diet of rats resulted in a significant increase in dipeptidase activity in the mucosa of the small intestine. There was no change in the mucosal weight in the intestinal segments or in the fractional incorporation of thymidine into mucosal cells. This effect on enzyme activity may help explain some of the observations on the action of avoparcin in the small intestine. Key words: Avoparcin, small intestine, dipeptidase, rat


2001 ◽  
Vol 120 (5) ◽  
pp. A183-A183
Author(s):  
H KOBAYASHI ◽  
H NAGATA ◽  
S MIURA ◽  
T AZUMA ◽  
H SUZUKI ◽  
...  

2008 ◽  
Vol 29 (S 1) ◽  
Author(s):  
K Nieber ◽  
S Michael ◽  
K Grötzinger ◽  
JW Rauwald ◽  
O Kelber

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