Wheat Germ Agglutinin and Dehydrins as ABA-Regulated Components of SA-Induced Cadmium Resistance in Wheat Plants

2017 ◽  
pp. 77-96 ◽  
Author(s):  
F. M. Shakirova ◽  
M. V. Bezrukova ◽  
Ch. R. Allagulova ◽  
D. R. Maslennikova ◽  
A. R. Lubyanova
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Cadmium Resistance

Failure of 6D1 or Exposure of Platelets to ADP to Affect Agglutination Induced by Wheat Germ Agglutinin

1989 ◽  
Vol 62 (02) ◽  
pp. 815 ◽  
Author(s):  
Marjorie B Zucker ◽  
Robert A Grant ◽  
Evelyn A Mauss
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ

Transport Characteristics of Wheat Germ Agglutinin-Modified Insulin-Liposomes and Solid Lipid Nanoparticles in a Perfused Rat Intestinal Model

2006 ◽  
Vol 6 (9) ◽  
pp. 2959-2966 ◽  
Author(s):  
Na Zhang ◽  
Qineng Ping ◽  
Guihua Huang ◽  
Xiuzhen Han ◽  
Yanna Cheng ◽  
...  
Keyword(s):  
Solid Lipid Nanoparticles ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Serum Insulin ◽  
Lipid Nanoparticles ◽  
Solid Lipid ◽  
Mucosal Absorption ◽  
Perfusion Experiment ◽  
Absorption Sites

Wheat germ agglutinin (WGA) modified liposomes and solid lipid nanoparticles (SLNs) were evaluated for improving intestinal absorption of insulin. In an in situ local intestinal perfusion experiment, formulations containing 100 IU/kg insulin were administered to the duodenum, jejunum, and ileum of fasted rats. As hypothesized, ileum was the best intestinal location for the absorption of insulin-containing liposomes. Serum insulin concentrations decreased for the various formulations in different absorption sites according to the following trends: Duodenum > ileum > jejunum for WGA-modified insulin-containing liposomes; duodenum > jejunum > ileum for WGA-modified insulin-containing SLNs; ileum > jejunum > duodenum for insulin-containing liposomes; ileum > duodenum > jejunum for insulin-containing SLNs; and duodenum ≥ ileum > jejunum for aqueous solution of insulin. These results imply that the nanoparticle type and delivery site were important factors with respect to increasing the bioavailability of insulin following oral administration. The proteolytic degradation as well as the epithelial permeability were primary determinants influcing insulin mucosal absorption.

Identification of distinct haemocyte populations from the freshwater bivalves swan mussel (Anodonta cygnea) and duck mussel (Anodonta anatina) using wheat-germ agglutinin

2017 ◽  
Vol 95 (12) ◽  
pp. 937-947 ◽  
Author(s):  
M. Hinzmann ◽  
M. Lopes-Lima ◽  
F. Cerca ◽  
A. Correia ◽  
J. Machado ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Transmission Microscopy ◽  
Anodonta Cygnea ◽  
Functional Studies ◽  
Lectin Staining ◽  
Surface Staining ◽  
Cytological Features ◽  
Freshwater Bivalves

Haemocytes play a major role in molluscs immunity. Functional studies are, however, impaired by limited available experimental tools to identify and sort distinct haemocyte populations. Therefore, using nonlethal methods, we aimed at evaluating whether lectin staining combined with flow cytometry could be used to distinguish circulating haemocyte populations from two freshwater bivalves of the family Unionidae, the duck mussel (Anodonta anatina (L., 1758)) and the swan mussel (Anodonta cygnea (L., 1758)). Based on classical classification, haemocytes were distinguished as granulocytes and hyalinocytes and cytological features were visualized using transmission microscopy and staining techniques. Size, granularity, viability, and surface staining using lectins as specific probes were analysed by flow cytometry and fluorescence microscopy. The microscopic proportions of granulocytes and hyalinocytes significantly differed, being of 70% and 30% for A. cygnea and of 85% and 15% for A. anatina, respectively. Two haemocyte populations were sorted by flow cytometry based on size and granularity and confirmed as granulocytes and hyalinocytes. Interestingly, two different granulocyte populations could be further discriminated in A. cygnea according to their binding affinity to wheat-germ agglutinin (WGA), whereas granulocytes of A. anatina all stained similarly. Our results show that WGA labelling combined with flow cytometry can be used to better discriminate Anodonta haemocyte populations and obtain purified populations for functional studies.

Protein phosphorylation and activation of platelets by wheat germ agglutinin

1985 ◽  
Vol 132 (1) ◽  
pp. 313-319 ◽  
Author(s):  
Chhanda L. Ganguly ◽  
Mohanathasan Chelladurai ◽  
Pankaj Ganguly
Keyword(s):  
Protein Phosphorylation ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ

Hevein-like domain IV in wheat germ agglutinin (WGA) is responsible for the majority of IgE cross-reactivity between WGA and hevein (Hev b 6.02)

2003 ◽  
Vol 111 (2) ◽  
pp. S327
Author(s):  
P. Karisola ◽  
H. Alenius ◽  
K. Turjanmaa ◽  
T. Reunala ◽  
N. Kalkkinen ◽  
...  
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Cross Reactivity
Sign in / Sign up

Export Citation Format

Share Document