Evidence of a specialized transport mechanism for the intestinal absorption of baclofen

1989 ◽  
Vol 10 (3) ◽  
pp. 279-297 ◽  
Author(s):  
M. Merino ◽  
J. E. Peris-Ribera ◽  
F. Torres-Molina ◽  
A. Sánchez-Picó ◽  
M. C. Garćia-Carbonell ◽  
...  
1959 ◽  
Vol 197 (1) ◽  
pp. 9-12 ◽  
Author(s):  
C. M. Paine ◽  
Howard J. Newman ◽  
M. Wight Taylor

Intestinal absorption of methionine and histidine was studied in adult chickens having permanent Thiry-Vella fistulas. The l isomers of both amino acids were absorbed from the fistulas more rapidly than were the d isomers. At a concentration of 10–3 m, 2,4-dinitrophenol retarded absorption of l-methionine but not of the d form. The absorption of l-histidine was impaired in the presence of equimolar concentrations of either l- or d-methionine. Racemization of d-methionine during absorption could not be demonstrated. The l isomers of both methionine and histidine appear to be absorbed from the chicken intestine by a common specific transport mechanism, with d-methionine being able to participate in at least one stage of this mechanism.


Author(s):  
John L. Beggs ◽  
John D. Waggener ◽  
Wanda Miller

Microtubules (MT) are versatile organelles participating in a wide variety of biological activity. MT involvement in the movement and transport of cytoplasmic components has been well documented. In the course of our study on trauma-induced vasogenic edema in the spinal cord we have concluded that endothelial vesicles contribute to the edema process. Using horseradish peroxidase as a vascular tracer, labeled endothelial vesicles were present in all situations expected if a vesicular transport mechanism was in operation. Frequently,labeled vesicles coalesced to form channels that appeared to traverse the endothelium. The presence of MT in close proximity to labeled vesicles sugg ested that MT may play a role in vesicular activity.


Author(s):  
Shou-kong Fan

Transmission and analytical electron microscopic studies of scale microstructures and microscopic marker experiments have been carried out in order to determine the transport mechanism in the oxidation of Ni-Al alloy. According to the classical theory, the oxidation of nickel takes place by transport of Ni cations across the scale forming new oxide at the scale/gas interface. Any markers deposited on the Ni surface are expected to remain at the scale/metal interface after oxidation. This investigation using TEM transverse section techniques and deposited microscopic markers shows a different result,which indicates that a considerable amount of oxygen was transported inward. This is the first time that such fine-scale markers have been coupled with high resolution characterization instruments such as TEM/STEM to provide detailed information about evolution of oxide scale microstructure.


1958 ◽  
Vol 34 (5) ◽  
pp. 901-909 ◽  
Author(s):  
Ervin Kaplan ◽  
Bernard D. Edidin ◽  
Robert C. Fruin ◽  
Lyle A. Baker

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