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A chitotetrose specific lectin fromLuffa acutangula: Physico-chemical properties and the assignment of orientation of sugars in the lectin binding site

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot

A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding

inferredcites →https://doi.org/10.1007/978-1-4684-0949-9_6openalex-snapshot

Studies on the Interaction of Concanavalin A with Glycoproteins

inferredcites →https://doi.org/10.1016/0003-2697(74)90139-0openalex-snapshot

A simplified method for cyanogen bromide activation of agarose for affinity chromatography

inferredcites →https://doi.org/10.1016/0005-2736(70)90265-8openalex-snapshot

Specific inhibition by N-acetyl-d-galactosamine of the interaction between soybean agglutinin and animal cell surfaces

inferredcites →https://doi.org/10.1016/0005-2795(78)90066-1openalex-snapshot

Circular dichroism studies on the effects of sodium dodecyl sulfate on the conformation of some phytohemagglutinins

inferredcites →https://doi.org/10.1016/0926-6526(64)90001-1openalex-snapshot

The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular-weight substrate for lysozyme

inferredcites →https://doi.org/10.1016/s0021-9258(17)32797-7openalex-snapshot

Lectin purification on affinity columns containing reductively aminated disaccharides.

inferredcites →https://doi.org/10.1016/s0021-9258(18)50686-4openalex-snapshot

The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid.

inferredcites →https://doi.org/10.1016/s0021-9258(18)94333-4openalex-snapshot

The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

inferredcites →https://doi.org/10.1016/s0021-9258(18)95955-7openalex-snapshot

A New Calibration Procedure for Gel Filtration Columns

inferredcites →https://doi.org/10.1016/s0021-9258(18)99551-7openalex-snapshot

The Binding of Oligosaccharides Containing N-Acetylglucosamine and N-Acetylmuramic Acid to Lysozyme

inferredcites →https://doi.org/10.1016/s0021-9258(20)79875-3openalex-snapshot

Structure of the O-Glycosidically Linked Carbohydrate Units of Fetuin

inferredcites →https://doi.org/10.1016/s0065-2318(08)60220-6openalex-snapshot

The Lectins: Carbohydrate-Binding Proteins of Plants and Animals

inferredcites →https://doi.org/10.1021/bi00504a006openalex-snapshot

Estimation of globular protein secondary structure from circular dichroism

inferredcites →https://doi.org/10.1021/bi00891a003openalex-snapshot

Equilibrium Ultracentrifugation of Dilute Solutions*

inferredcites →https://doi.org/10.1038/257802a0openalex-snapshot

Interaction between lectin from Ricinus communis and liposomes containing gangliosides

inferredcites →https://doi.org/10.1042/bj1310155openalex-snapshot

The purification, composition and specificity of wheat-germ agglutinin

inferredcites →https://doi.org/10.1042/bj1830133openalex-snapshot

A lectin from the exudate of the fruit of the vegetable marrow (Cucurbita pepo) that has a specificity for β-1,4-linked N-acetylglucosamine oligosaccharides

inferredcites →https://doi.org/10.1042/bj1970345openalex-snapshot

Some properties of the lectin from Datura stramonium (thorn-apple) and the nature of its glycoprotein linkages

inferredcites →https://doi.org/10.1080/00327487808069054openalex-snapshot

A Large Scale Preparation op Peanut Agglutinin on a New Affinity Matrix

inferredcites →https://doi.org/10.1111/j.1432-1033.1974.tb03468.xopenalex-snapshot

On the Specificity of Carbohydrate‐Lectin Recognition

inferredcites →https://doi.org/10.1111/j.1432-1033.1978.tb12092.xopenalex-snapshot

Binding of 4-Methylumbelliferyl alpha-Manno-oligosaccharides to Concanavalin A: Equilibrium Study

inferredcites →https://doi.org/10.1111/j.1432-1033.1980.tb04410.xopenalex-snapshot

Sugar‐Lectin Interactions: How Does Wheat‐Germ Agglutinin Bind Sialoglycoconjugates?

inferredcites →https://doi.org/10.1146/annurev.bi.42.070173.002545openalex-snapshot

The Biochemistry of Plant Lectins (Phytohemagglutinins)

inferredcites →https://doi.org/10.1146/annurev.bi.50.070181.001231openalex-snapshot

Lectins: Their Multiple Endogenous Cellular Functions

inferredcites →https://doi.org/10.1146/annurev.pp.27.060176.001451openalex-snapshot

Phytohemagglutinins (Phytolectins)

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.phytochem.2022.113251zenodo-depositor-declared

Cucurbitaceae phloem exudate lectins: Purification, molecular characterization and carbohydrate binding characteristics

inferred← citeshttps://doi.org/10.1007/978-3-032-15466-8_17openalex-snapshot

Luffa acutangula (L.) Roxb.

inferred← citeshttps://doi.org/10.1007/978-94-007-1764-0_45openalex-snapshot

Luffa acutangula

inferred← citeshttps://doi.org/10.1007/s10719-010-9305-2openalex-snapshot

Mutational analysis of the carbohydrate binding activity of the tobacco lectin

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.10.078openalex-snapshot

Purification, physico-chemical characterization and thermodynamics of chitooligosaccharide binding to cucumber (Cucumis sativus) phloem lectin

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2019.06.211openalex-snapshot

Chitooligosaccharide binding to CIA17 (Coccinia indica agglutinin). Thermodynamic characterization and formation of higher order complexes

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.08.246openalex-snapshot

Purification, biochemical/biophysical characterization and chitooligosaccharide binding to BGL24, a new PP2-type phloem exudate lectin from bottle gourd (Lagenaria siceraria)

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