Arabinogalactan-proteins in roots of Echinacea purpurea: Structural investigations and microscopic localization by immunofluorescent labelling

Planta Medica ◽  
2007 ◽  
Vol 73 (09) ◽  
Author(s):  
A Bossy ◽  
W Blaschek ◽  
B Classen
Keyword(s):  
Echinacea Purpurea ◽  
Arabinogalactan Proteins ◽  
Structural Investigations ◽  
Microscopic Localization

Interaction of lectin from Viscum album L. with arabinogalactan-proteins from Echinacea purpurea (L.) Moench

2008 ◽  
Vol 29 (S 1) ◽  
Author(s):  
B Classen ◽  
B Herbst ◽  
W Blaschek ◽  
K Pfüller ◽  
U Pfüller
Keyword(s):  
Echinacea Purpurea ◽  
Viscum Album ◽  
Arabinogalactan Proteins

scholarly journals Degraded Arabinogalactans and Their Binding Properties to Cancer-Associated Human Galectins

2021 ◽  
Vol 22 (8) ◽  
pp. 4058
Author(s):  
Lukas Pfeifer ◽  
Alexander Baumann ◽  
Lea Madlen Petersen ◽  
Bastian Höger ◽  
Eric Beitz ◽  
...  
Keyword(s):  
Zostera Marina ◽  
Echinacea Purpurea ◽  
Arabinogalactan Proteins ◽  
Uronic Acids ◽  
Binding Properties ◽  
Free System ◽  
Plant Polysaccharides ◽  
Kd Values ◽  
A Cell ◽  
Partial Degradation

Galectins represent β-galactoside-binding proteins with numerous functions. Due to their role in tumor progression, human galectins-1, -3 and -7 (Gal-1, -3 and -7) are potential targets for cancer therapy. As plant derived glycans might act as galectin inhibitors, we prepared galactans by partial degradation of plant arabinogalactan-proteins. Besides commercially purchased galectins, we produced Gal-1 and -7 in a cell free system and tested binding capacities of the galectins to the galactans by biolayer-interferometry. Results for commercial and cell-free expressed galectins were comparable confirming functionality of the cell-free produced galectins. Our results revealed that galactans from Echinacea purpurea bind to Gal-1 and -7 with KD values of 1–2 µM and to Gal-3 slightly stronger with KD values between 0.36 and 0.70 µM depending on the sensor type. Galactans from the seagrass Zostera marina with higher branching of the galactan and higher content of uronic acids showed stronger binding to Gal-3 (0.08–0.28 µM) compared to galactan from Echinacea. The results contribute to knowledge on interactions between plant polysaccharides and galectins. Arabinogalactan-proteins have been identified as a new source for production of galactans with possible capability to act as galectin inhibitors.

Observation of biological macromolecules using various electron microscopic methods

1978 ◽  
Vol 36 (2) ◽  
pp. 170-171
Author(s):  
Mitsuo Ohtsuki ◽  
Michael Sogard
Keyword(s):  
Electron Microscope ◽  
Phase Contrast ◽  
Image Interpretation ◽  
Density Lipoprotein ◽  
Biological Macromolecules ◽  
Contrast Effects ◽  
Biological Structure ◽  
Electron Microscopic ◽  
Structural Investigations ◽  
Staining Techniques

Structural investigations of biological macromolecules commonly employ CTEM with negative staining techniques. Difficulties in valid image interpretation arise, however, due to problems such as variability in thickness and degree of penetration of the staining agent, noise from the supporting film, and artifacts from defocus phase contrast effects. In order to determine the effects of these variables on biological structure, as seen by the electron microscope, negative stained macromolecules of high density lipoprotein-3 (HDL3) from human serum were analyzed with both CTEM and STEM, and results were then compared with CTEM micrographs of freeze-etched HDL3. In addition, we altered the structure of this molecule by digesting away its phospholipid component with phospholipase A2 and look for consistent changes in structure.

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