Biological effects and chemical characterization of Iris schachtii Markgr. extracts: A new source of bioactive constituents

2018 ◽  
Vol 112 ◽  
pp. 448-457 ◽  
Author(s):  
Andrei Mocan ◽  
Gokhan Zengin ◽  
Adriano Mollica ◽  
Ahmet Uysal ◽  
Erdogan Gunes ◽  
...  
Chemosphere ◽  
2013 ◽  
Vol 90 (2) ◽  
pp. 611-619 ◽  
Author(s):  
S. Chamorro ◽  
V. Hernández ◽  
V. Matamoros ◽  
C. Domínguez ◽  
J. Becerra ◽  
...  

2017 ◽  
Vol 31 (10) ◽  
pp. e21941 ◽  
Author(s):  
Andrea B. Pizzo ◽  
Renê O. Beleboni ◽  
Ruither O. Gomes Carolino ◽  
Luciana de Oliveira ◽  
Antonio Miranda ◽  
...  

2019 ◽  
Vol 44 (1) ◽  
Author(s):  
Xiao Tian ◽  
Sen Guo ◽  
Shanshan Zhang ◽  
Peisheng Li ◽  
Tianyi Wang ◽  
...  

2001 ◽  
Vol 12 (9) ◽  
pp. 2825-2834 ◽  
Author(s):  
Hanan Osman ◽  
Sébastien Vauthrin ◽  
Vladimir Mikes ◽  
Marie-Louise Milat ◽  
Franck Panabières ◽  
...  

Elicitins secreted by phytopathogenic Phytophthoraspp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionality. However, these proteins were strongly altered in their sterol-loading efficiency, specific binding to high-affinity sites, and activities on tobacco cells. Ligand replacement experiments strongly suggest that the formation of a sterol-elicitin complex is a requisite step before elicitins fasten to specific binding sites. This was confirmed with the use of two sterol-preloaded elicitins. Both more rapidly displaced labeled cryptogein from its specific binding sites than the unloaded proteins. Moreover, the binding kinetics of elicitins are related to their biological effects, which constitutes the first evidence that binding sites could be the biological receptors. The first event involved in elicitin-mediated cell responses is proposed to be the protein loading with a sterol molecule.


2016 ◽  
Vol 7 (6) ◽  
pp. 2870-2877 ◽  
Author(s):  
Lu Bai ◽  
Hai Zhang ◽  
Qingchao Liu ◽  
Yong Zhao ◽  
Xueqin Cui ◽  
...  

The fruit of Ziziphus jujuba Mill., also called hongzao in Chinese, has a long history of cultivation in China.


1981 ◽  
Author(s):  
Birgitta Berglund ◽  
Ulf Berglund ◽  
Thomas Lindvall ◽  
Helene Nicander-Bredberg

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.


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