Immunohistochemical Localization of Metallothionein in Organs of Rats Treated with either Cadmium, Inorganic or Organic Mercurials

1991 ◽  
pp. 155-165 ◽  
Author(s):  
Chiharu Tohyama ◽  
Abdul Ghaffar ◽  
Atsuhiro Nakano ◽  
Noriko Nishimura ◽  
Hisao Nishimura
1999 ◽  
Vol 19 (3) ◽  
pp. 302-310
Author(s):  
Yukihiko Kohda ◽  
Katsuhiro Tsuchiya ◽  
Junkoh Yamashita ◽  
Masaki Yoshida ◽  
Takashi Ueno ◽  
...  

1998 ◽  
Vol 5 (1) ◽  
pp. 137A-137A
Author(s):  
J MCCARTHY ◽  
D MISRA ◽  
A KANBOURSHAKIR ◽  
L MINICH ◽  
D LYKINS ◽  
...  

1989 ◽  
Vol 120 (3_Suppl) ◽  
pp. S202-S203
Author(s):  
G. WESTHOF ◽  
J. BENSCH ◽  
W. L. BRAENDLE

Biomics ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 329-336
Author(s):  
A.R. Lubyanova ◽  
F.M. Shakirova ◽  
M.V. Bezrukova

We studied the immunohistochemical localization of abscisic acid (ABA), wheat germ agglutinin (WGA) and dehydrins in the roots of wheat seedlings (Triticum aestivum L.) during 24-epibrassinolide-pretreatment (EB-pretreatment) and PEG-induced dehydration. It was found coimmunolocalization of ABA, WGA and dehydrins in the cells of central cylinder of basal part untreated and EB-pretreated roots of wheat seedlings under normal conditions and under osmotic stress. Such mutual localization ABA and protective proteins, WGA and dehydrins, indicates the possible effect of their distribution in the tissues of EB-pretreated wheat roots during dehydration on the apoplastic barrier functioning, which apparently contributes to decrease the water loss under dehydration. Perhaps, the significant localization of ABA and wheat lectin in the metaxylem region enhances EB-induced transport of ABA and WGA from roots to shoots under stress. It can be assumed that brassinosteroids can serve as intermediates in the realization of the protective effect of WGA and wheat dehydrins during water deficit.


2012 ◽  
Vol 48 (No. 12) ◽  
pp. 369-372
Author(s):  
S. Timurkaan ◽  
A. Aydin ◽  
M. Kaban

The localization of calbindin in the kidney and cerebellum of Hystrix cristata was investigated immu­nohistochemically using an antiserum against the 28k Da calbindin of chicken duodenum. Calbindin-D28k is an intracellular protein with a high affinity for calcium. This protein is exclusively localized in the distal convoluted tubules of the kidney and in Purkinje cells of the cerebellum. Functionaly, calbindin-D28k is supposed to be involved in the regulation of the reabsorption of calcium in the distal nephron, though the exact regulatory mechanisms are not yet known.


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