scholarly journals Identification of ABCC2 as a binding protein of Cry1Ac on brush border membrane vesicles from Helicoverpa armigera by an improved pull‐down assay

2016 ◽  
Vol 5 (4) ◽  
pp. 659-669 ◽  
Author(s):  
Zishan Zhou ◽  
Zeyu Wang ◽  
Yuxiao Liu ◽  
Gemei Liang ◽  
Changlong Shu ◽  
...  
PROTEOMICS ◽  
2010 ◽  
Vol 10 (24) ◽  
pp. 4431-4440 ◽  
Author(s):  
Santosh Kumar Upadhyay ◽  
Manisha Mishra ◽  
Harpal Singh ◽  
Amol Ranjan ◽  
Krishnappa Chandrashekar ◽  
...  

1988 ◽  
Vol 59 (3) ◽  
pp. 497-507 ◽  
Author(s):  
Dallynn. Salter ◽  
Peter Blakeborough

1. The influence of goat's-milk folate-binding protein (FBP) on the uptake of 5-methyltetrahydrofolate (MTHF) by brush-border-membrane vesicles prepared from the small intestine of the 6-d-old goat was investigated using a rapid-filtration assay.2. Uptake of MTHF by the membrane vesicles was strongly enhanced by FBP within the pH range 4·5-6·5, with an optimum at pH 5-5·5.3. Both the initial rate of MTHF uptake and uptake of MTHF at equilibrium were markedly increased in the presence of FBP.4. Uptake of MTHF by brush-border-membrane vesicles was maximal when the molar ratio FBP: MTHF was 1·0-2·5.5. The relation between pH and 125I-labelled FBP binding to the membranes was similar to that for uptake of MTHF, with an optimum at pH 5.6. In experiments in which the osmotic pressure of the incubation medium was progressively increased with cellobiose, 125I-labelled FBP was found to be taken up primarily by binding to the brush-border-membrane surface.7. Uptake of 125I-labelled FBP was time-dependent and saturable, with a Km of 0·39 (SE 0·07) μM and Vmax of 6·73 (SE 0·92) μg/mg protein.8. Experiments in which various milk proteins (cow FBP, goat FBP, α-lactalbumin, β-lactoglobulin, bovine serum albumin and lactoferrin) were allowed to compete in turn with 125I-labelled FBP for uptake by brush-border-membrane vesicles indicated that high-affinity binding was probably specific to FBP, although lactoferrin reduced uptake possibly by non-specific coating of the mucosal surface.9. It was concluded that a folate transport mechanism mediated by the FBP in milk exists at the intestinal brush border of neonatal goats. It is suggested that this may reinforce the developing endogenous transport system.


1989 ◽  
Vol 257 (5) ◽  
pp. C971-C975 ◽  
Author(s):  
H. A. Skopicki ◽  
K. Fisher ◽  
D. Zikos ◽  
G. Flouret ◽  
D. R. Peterson

These studies were performed to determine if a low-affinity carrier is present in the luminal membrane of proximal tubular cells for the transport of the dipeptide, pyroglutamyl-histidine (pGlu-His). We have previously described the existence of a specific, high-affinity, low-capacity [transport constant (Kt) = 9.3 X 10(-8) M, Vmax = 6.1 X 10(-12) mol.mg-1.min-1] carrier for pGlu-His in renal brush-border membrane vesicles. In the present study, we sought to demonstrate that multiple carriers exist for the transport of a single dipeptide by determining whether a low-affinity carrier also exists for the uptake of pGlu-His. Transport of pGlu-His into brush-border membrane vesicles was saturable over the concentration range of 10(-5)-10(-3) M, yielding a Kt of 6.3 X 10(-5) M and a Vmax of 2.2 X 10(-10) mol.mg-1.min-1. Uptake was inhibited by the dipeptides glycyl-proline, glycyl-sarcosine, and carnosine but not by the tripeptide pyroglutamyl-histidyl-prolinamide. We conclude that 1) pGlu-His is transported across the luminal membrane of the proximal tubule by multiple carriers and 2) the lower affinity carrier, unlike the higher affinity carrier, is nonspecific with respect to other dipeptides.


2021 ◽  
Vol 139 ◽  
pp. 109940
Author(s):  
Lesbia Cristina Julio-Gonzalez ◽  
F. Javier Moreno ◽  
María Luisa Jimeno ◽  
Elisa G. Doyagüez ◽  
Agustín Olano ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document