Exploring stress overshoot phenomenon upon startup deformation of entangled linear polymeric liquids

2009 ◽  
Vol 53 (6) ◽  
pp. 1389-1401 ◽  
Author(s):  
Yangyang Wang ◽  
Shi-Qing Wang

Soft Matter ◽  
2021 ◽  
Author(s):  
Aditya Natu ◽  
Uddipta Ghosh

Flow of polymeric liquids in narrow confinements of rectangular cross section, in the presence of electrical double layers is analyzed here. Our analysis is motivated by the fact that many...



1991 ◽  
Vol 260 (3) ◽  
pp. R563-R569 ◽  
Author(s):  
S. J. Reshkin ◽  
G. A. Ahearn

The transport mechanisms for the dipeptide glycyl-L-phenylalanine (Gly-Phe) and L-phenylalanine (Phe) were characterized in fish intestinal brush-border membrane vesicles (BBMV). Gly-Phe was rapidly hydrolyzed only intravesicularly with almost total hydrolysis occurring even at 10 s. Dipeptide uptake was not stimulated by an inward gradient of Na, K, or H. Phe uptake was stimulated by an inward gradient of either Na or K but displayed an overshoot phenomenon only in the presence of an Na gradient. Kinetic analysis of the effect of substrate concentration on transport rate revealed that transport of both Gly-Phe and Phe occurred by a saturable process conforming to Michaelis-Menten kinetics. The Km for Gly-Phe was 9.8 +/- 3.5 mM, whereas that for Phe in the presence of Na or K, respectively, was 0.74 +/- 0.13 and 1.1 +/- 0.37 mM. Maximum uptake for Gly-Phe and for Phe in the presence of Na and K was 5.1, 0.9, and 0.4 nmol.mg and protein-1.5 s-1, respectively. Gly-Phe and Phe transport displayed different patterns of inhibition by dipeptides and amino acids. These results suggest that Gly-Phe and Phe are transported via different mechanisms, with Gly-Phe being hydrolyzed during a carrier-mediated, cation-independent process and Phe being transferred via a Na+ cotransport process similar to that described in mammals. During conditions of high luminal dipeptide concentrations, the Gly-Phe pathway may make a significant contribution to total Phe uptake.



2015 ◽  
Vol 81 (823) ◽  
pp. 14-00612-14-00612 ◽  
Author(s):  
Mitsuhiro OHTA ◽  
Yasufumi HIEDA ◽  
Norihiko TOKUI ◽  
Shuichi IWATA


2000 ◽  
Vol 84 (21) ◽  
pp. 4858-4861 ◽  
Author(s):  
Miguel Aubouy ◽  
Manoel Manghi ◽  
Elie Raphaël


1989 ◽  
Vol 264 (1) ◽  
pp. 223-231 ◽  
Author(s):  
T C Williams ◽  
A J Doherty ◽  
D A Griffith ◽  
S M Jarvis

The transport of uridine into rabbit renal outer-cortical brush-border and basolateral membrane vesicles was compared at 22 degrees C. Uridine was taken up into an osmotically active space in the absence of metabolism for both types of membrane vesicles. Uridine influx by brush-border membrane vesicles was stimulated by Na+, and in the presence of inwardly directed gradients of Na+ a transient overshoot phenomenon was observed, indicating active transport. Kinetic analysis of the saturable Na+-dependent component of uridine flux indicated that it was consistent with Michaelis-Menten kinetics (Km 12 +/- 3 microM, Vmax. 3.9 +/- 0.9 pmol/s per mg of protein). The sodium:uridine coupling stoichiometry was found to be consistent with 1:1 and involved the net transfer of positive charge. In contrast, uridine influx by basolateral membrane vesicles was not dependent on the cation present and was inhibited by nitrobenzylthioinosine (NBMPR). NBMPR-sensitive uridine transport was saturable (Km 137 +/- 20 microM, Vmax. 5.2 +/- 0.6 pmol/s per mg of protein). Inhibition of uridine flux by NBMPR was associated with high-affinity binding of NBMPR to the basolateral membrane (Kd 0.74 +/- 0.46 nM). Binding of NBMPR to these sites was competitively blocked by adenosine and uridine. These results indicate that uridine crosses the brush-border surface of rabbit proximal renal tubule cells by Na+-dependent pathways, but permeates the basolateral surface by NBMPR-sensitive facilitated-diffusion carriers.





2020 ◽  
Vol 23 (2) ◽  
pp. 23801
Author(s):  
Shrivastav ◽  
Kahl
Keyword(s):  




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