scholarly journals Wheat (Triticum aestivum L.) selenium-binding protein-A enhances cadmium tolerance via interaction between CXXC motif and cadmium and detoxification

2020 ◽  
Author(s):  
Fei Luo ◽  
Dong Zhu ◽  
Rong Zou ◽  
Wenjing Duan ◽  
Yueming Yan
Keyword(s):  
Triticum Aestivum ◽  
Binding Protein ◽  
Protein A ◽  
Triticum Aestivum L ◽  
Cadmium Tolerance ◽  
Cxxc Motif

Immunocytochemical localization of wheat prolamins in the lumen of the rough endoplasmic reticulum

1991 ◽  
Vol 69 (11) ◽  
pp. 2574-2577 ◽  
Author(s):  
Hari B. Krishnan ◽  
Jerry A. White ◽  
Steven G. Pueppke
Keyword(s):  
Triticum Aestivum ◽  
Endoplasmic Reticulum ◽  
Key Words ◽  
Rough Endoplasmic Reticulum ◽  
Protein A ◽  
Triticum Aestivum L ◽  
Soluble Proteins ◽  
Immunocytochemical Localization ◽  
Specific Antibodies ◽  
Days After Anthesis

Antibodies raised against gliadins, the alcohol-soluble proteins of wheat (Triticum aestivum L.) seeds, were used to localize gliadins within the lumen of the endoplasmic reticulum. Endosperm cells at 20 days after anthesis contain extensive rough endoplasmic reticulum that is fragmented and dilated. The dilated endoplasmic reticulum encloses aggregates of proteinaceous material that reacts strongly with gliadin-specific antibodies. Key words: gliadins, immunocytochemistry, protein A – gold, rough endoplasmic reticulum, wheat.

Root characteristics critical for cadmium tolerance and reduced accumulation in wheat (Triticum aestivum L.)

2022 ◽  
Vol 305 ◽  
pp. 114365
Author(s):  
Dazhong Zhang ◽  
Hao Zhou ◽  
Leilei Shao ◽  
Hairong Wang ◽  
Yuanbo Zhang ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Triticum Aestivum L ◽  
Cadmium Tolerance ◽  
Root Characteristics

Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum
Keyword(s):  
Actin Filaments ◽  
High Speed ◽  
Binding Protein ◽  
Protein A ◽  
Actin Binding ◽  
Platelet Glycoprotein ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Triton X ◽  
Calpain Inhibitors

SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP interaction resides in the 90 kDa region of ABP. GP lb was sedimented with the Triton-insoluble actin filaments in trace amounts only, and only after high speed centrifugation (100,000 × g, 3 h). Both the 190 kDa and the 90 kDa fragments of ABP were sedimented with the Triton-insoluble actin filaments.

ИЗОФЕРМЕНТНЫЙ АНАЛИЗ ЭСТЕРАЗ В ЗРЕЛЫХ СЕМЕНАХ ГЕКСАПЛОИДНОЙ МЯГКОЙ ПШЕНИЦЫ (Triticum aestivum L.)

2016 ◽  
Vol 51 (3) ◽  
pp. 327-334
Author(s):  
А.С. РУДАКОВА ◽  
◽  
С.В. РУДАКОВ ◽  
Н.В. ДАВЫДОВА ◽  
Г.В. МИРСКАЯ ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Triticum Aestivum L
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