scholarly journals Isolation and partial characterization of an N-acetylgalactosamine-specific lectin from winter-aconite (Eranthis hyemalis) root tubers

1985 ◽  
Vol 227 (3) ◽  
pp. 949-955 ◽  
Author(s):  
B P Cammue ◽  
B Peeters ◽  
W J Peumans
Keyword(s):  
Glutamic Acid ◽  
Affinity Chromatography ◽  
Blood Group ◽  
Carbohydrate Binding ◽  
Plant Family ◽  
Binding Properties ◽  
Plant Lectins ◽  
Disulphide Bonds ◽  
Dimeric Protein

A lectin was isolated from root tubers of winter aconite (Eranthis hyemalis) by affinity chromatography on fetuin-agarose, and it was partially characterized with respect to its biochemical, physicochemical and carbohydrate-binding properties. The Eranthis hyemalis lectin is a dimeric protein (Mr 62000) composed of two different subunits of Mr 30000 and 32000, held together by disulphide bonds. It is especially rich in asparagine/aspartic acid, glutamine/glutamic acid and leucine, and contains 5% covalently bound carbohydrate. Hapten inhibition assays indicated that the winter-aconite lectin is specific for N-acetylgalactosamine. In addition, the lectin exhibits a pronounced specificity towards blood-group-O erythrocytes. The winter-aconite lectin is the first lectin to be isolated from a species belonging to the plant family Ranunculaceae. It appears to be different from all previously described plant lectins.

scholarly journals Studies on Lectin Mediated Agglutination Reaction on Red Blood Cell Surface Antigens Using Hot and Cold Water Plant Extracts

2021 ◽  
pp. 48-52
Author(s):  
Bhavya Sahithi Velagapudi ◽  
Hemanth Sai Nannapaneni ◽  
Akanksha Alampally ◽  
Suryanarayana Veeravilli ◽  
Duggipogu Praveen Kumar ◽  
...  
Keyword(s):  
Cold Water ◽  
Surface Protein ◽  
Hot Water ◽  
Carbohydrate Binding ◽  
Cell Surface Antigens ◽  
Binding Properties ◽  
Cell Agglutination ◽  
Plant Lectins ◽  
Water Plant

Lectin has various physiological roles in cell agglutination, based on their carbohydrate-binding properties, plant lectins are widely used for the detection, segregation, and characterization of glycoconjugates. Rhesus (Rh) factor is a protein that is inherited and found on the surface of red blood cells. If the surface protein is present, the RBC is Rh positive; otherwise, it is Rh-negative in nature. In this paper, we use agglutination reactions to investigate the effect of different cold and hot water extracted plants on RBC antigens as an alternative to commercial monoclonal antibodies. Extensive research on the sequence homology and 3-D structure of various plant lectins suggests that they have been conserved throughout evolution and may play important physiological roles that are still unknown.

scholarly journals Identification of carbohydrate-binding proteins from mouse and human fibroblasts

1983 ◽  
Vol 211 (3) ◽  
pp. 625-629 ◽  
Author(s):  
C F Roff ◽  
P R Rosevear ◽  
J L Wang ◽  
R Barker
Keyword(s):  
Affinity Chromatography ◽  
Binding Proteins ◽  
Human Fibroblasts ◽  
Carbohydrate Binding ◽  
Binding Properties ◽  
3T3 Fibroblasts ◽  
Mouse Protein ◽  
Human Foreskin Fibroblasts ◽  
Human Counterpart ◽  
Carbohydrate Binding Proteins

Three carbohydrate-binding proteins (Mr 35 000, 16 000 and 13 500) were isolated from extracts of mouse 3T3 fibroblasts by affinity chromatography on polyacrylamide beads to which was covalently bound the ligand 6-aminohexyl 4-beta-D-galactosyl-2-acetamido-2-deoxy-beta-D-glucopyranoside. None of these proteins bind to polyacrylamide beads coupled with either 6-aminohexanol or 6-aminohexyl β-D-galactopyranoside. Therefore they appear to be carbohydrate-binding proteins specific for galactose-terminated glycoconjugates. A carbohydrate-binding protein was also purified from extracts of human foreskin fibroblasts. This protein (Mr 35000) may represent the human counterpart of the mouse protein of similar Mr and binding properties.

scholarly journals A lectin from elder (Sambucus nigra L.) bark

1984 ◽  
Vol 221 (1) ◽  
pp. 163-169 ◽  
Author(s):  
W F Broekaert ◽  
M Nsimba-Lubaki ◽  
B Peeters ◽  
W J Peumans
Keyword(s):  
Glutamic Acid ◽  
Affinity Chromatography ◽  
Aspartic Acid ◽  
Sambucus Nigra ◽  
Plant Family

A lectin was isolated from elder (Sambucus nigra) bark by affinity chromatography on fetuin-agarose. It is a tetrameric molecule (Mr 140000) composed of two different subunits of Mr 34500 and 37500 respectively, held together by intramolecular disulphide bridges. The lectin is a glycoprotein and is especially rich in asparagine/aspartic acid, glutamine/glutamic acid, valine and leucine. It is also the first lectin isolated from a species belonging to the plant family Caprifoliaceae.

scholarly journals Isolation and partial characterization of a lectin from a false brome grass (Brachypodium sylvaticum)

1982 ◽  
Vol 205 (3) ◽  
pp. 635-638 ◽  
Author(s):  
W J Peumans ◽  
C Spaepen ◽  
H M Stinissen ◽  
A R Carlier
Keyword(s):  
Physicochemical Properties ◽  
Affinity Chromatography ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Partial Characterization ◽  
Grass Species ◽  
Brachypodium Sylvaticum ◽  
Dimeric Protein ◽  
Brome Grass

A lectin has been isolated from embryos of a false brome grass species (Brachypodium sylvaticum) by affinity chromatography on immobilized N-acetylglucosamine. It is a dimeric protein of two identical subunits of mol.wt. 18 000. Although it resembles cereal lectins with respect to its biochemical and physicochemical properties, it differs structurally in several aspects from wheat-germ-agglutinin-like lectins.

scholarly journals Isolation and partial characterization of a lectin from Euphorbia heterophylla seeds

1983 ◽  
Vol 215 (1) ◽  
pp. 141-145 ◽  
Author(s):  
M Nsimba-Lubaki ◽  
W J Peumans ◽  
A R Carlier
Keyword(s):  
Affinity Chromatography ◽  
Partial Characterization ◽  
Dimeric Protein

An N-acetylgalactosamine-specific lectin was isolated from Euphorbia heterophylla seeds by affinity chromatography on cross-linked arabinogalactan. It is a dimeric protein of two identical subunits of Mr 32 000, and differs structurally from all previously known Euphorbiaceae lectins. Its distribution over the seed is typical in that it is merely confined to the primary axes.

Mechanism of chitosan recognition by CBM32 carbohydrate-binding modules from a Paenibacillus sp. IK-5 chitosanase/glucanase

2016 ◽  
Vol 473 (8) ◽  
pp. 1085-1095 ◽  
Author(s):  
Shoko Shinya ◽  
Shigenori Nishimura ◽  
Yoshihito Kitaoku ◽  
Tomoyuki Numata ◽  
Hisashi Kimoto ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Binding Site ◽  
Carbohydrate Binding ◽  
Binding Properties ◽  
Fungal Cell ◽  
Mutant Proteins ◽  
Loop Region ◽  
C Terminus ◽  
Carbohydrate Binding Modules ◽  
Paenibacillus Sp

An antifungal chitosanase/glucanase isolated from the soil bacterium Paenibacillus sp. IK-5 has two CBM32 chitosan-binding modules (DD1 and DD2) linked in tandem at the C-terminus. In order to obtain insights into the mechanism of chitosan recognition, the structures of DD1 and DD2 were solved by NMR spectroscopy and crystallography. DD1 and DD2 both adopted a β-sandwich fold with several loops in solution as well as in crystals. On the basis of chemical shift perturbations in 1H-15N-HSQC resonances, the chitosan tetramer (GlcN)4 was found to bind to the loop region extruded from the core β-sandwich of DD1 and DD2. The binding site defined by NMR in solution was consistent with the crystal structure of DD2 in complex with (GlcN)3, in which the bound (GlcN)3 stood upright on its non-reducing end at the binding site. Glu14 of DD2 appeared to make an electrostatic interaction with the amino group of the non-reducing end GlcN, and Arg31, Tyr36 and Glu61 formed several hydrogen bonds predominantly with the non-reducing end GlcN. No interaction was detected with the reducing end GlcN. Since Tyr36 of DD2 is replaced by glutamic acid in DD1, the mutation of Tyr36 to glutamic acid was conducted in DD2 (DD2-Y36E), and the reverse mutation was conducted in DD1 (DD1-E36Y). Ligand-binding experiments using the mutant proteins revealed that this substitution of the 36th amino acid differentiates the binding properties of DD1 and DD2, probably enhancing total affinity of the chitosanase/glucanase toward the fungal cell wall.

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