A Calcium Binding Component of Dog Kidney Cortex and Its Relationship to Calcium Transport

1971 ◽  
Vol 137 (4) ◽  
pp. 1267-1273 ◽  
Author(s):  
H. Sands ◽  
R. H. Kessler
Author(s):  
P.T. Nguyen ◽  
C. Uphoff ◽  
C.L. Stinemetz

Considerable evidence suggest that the calcium-binding protein calmodulin (CaM) may mediate calcium action and/or transport important in the gravity response of plants. Calmodulin is present in both shoots and roots and is capable of regulating calcium transport in plant vesicles. In roots calmodulin is concentrated in the tip, the gravisensing region of the root; and is reported to be closely associated with amyloplasts, organelles suggested to play a primary role in gravi-perception. Inhibitors of CaM such as chlorpromazine, calmidazolium, and compound 48/80 interfere with the gravitropic response of both snoots and roots. The magnitude of the inhibition corresponded well with the extent to which the drug binds to endogenous CaM. Compound 48/80 and calmidazolium block gravi-induced changes in electrical currents across root tips, a phenomenon thought to be associated with the sensing of the gravity stimulus.In this study, we have investigated the subcellular distribution of CaM in graviresponsive and non-graviresponsive root caps of the maize cultivar Merit.


1992 ◽  
Vol 297 (2) ◽  
pp. 213-220 ◽  
Author(s):  
Roberto Lara-Lemus ◽  
Carlos A. Libreros-Minotta ◽  
Myriam M. Altamirano ◽  
Mario L. Calcagno

FEBS Letters ◽  
1974 ◽  
Vol 47 (1) ◽  
pp. 76-80 ◽  
Author(s):  
P. Gmaj ◽  
C. Nowicka ◽  
S. Angielski

1978 ◽  
Vol 77 (3) ◽  
pp. 743-751 ◽  
Author(s):  
RS Tuan ◽  
WA Scott ◽  
ZA Cohn

The preparation of a specific antiserum (anti-CaBP) against the calcium-binding protein (CaBP) of the chorioallantoic membrane (CAM) is described. The anti-CaBP appeared to be specific for the CaBP by immunodiffusion and immunoelectrophoresis. Application of the anti-CaBP in immunofluorescence histochemistry revealed that the CaBP is present in the CAM only at developmental ages corresponding with the expression of the calcium transport function of the membrane. Furthermore, the CaBP is localized to the ectoderm of the CAM, appears to be exposed to the entire external surface of the ectoderm, and can be shown to be associated with cells enzymatically dissociated from the CAM. These results are consistent with a functional role of the CaBP in the CAM calcium transport process.


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