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Journal ArticleDOI

Agrocybe cylindracea lectin is a member of the galectin family.

Fumio Yagi, +2 more
- 01 Oct 2001 - 
- Vol. 18, Iss: 10, pp 745-749
TLDR
The complete amino acid sequence of Agrocybe cylindracea lectin was determined from the peptides obtained by chemical cleavages and enzymatic hydrolyses and several insertions suggest that β-strands S2, F3, and S4 and the loop structures between β-Strands F2 & S3 and F5 & S2 are different from those of galectins reported so far.
Abstract
The complete amino acid sequence of Agrocybe cylindracea lectin was determined from the peptides obtained by chemical cleavages and enzymatic hydrolyses. The sequence shows 19.1% and 36.8% identity with those of human galectin-1 and Coprinus lectin-1, a fungal galectin, respectively. Seven residues, which are commonly found in carbohydrate recognizing domain (CRD) of galectins, were conserved. However, several insertions in the sequence, compared with those of human galectin-1 and Coprinus lectin-1, suggest that β-strands S2, F3, and S4 and the loop structures between β-strands F2 & S3 and F5 & S2 are different from those of galectins reported so far.

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Citations
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Journal ArticleDOI

Molecular character of the recombinant antitumor lectin from the edible mushroom Agrocybe aegerita

TL;DR: The results reveal that AAL is a member of the galectin family and the dimeric form is the active unit for the functional performance and the molecular characters revealed by this study are significant for the in-depth investigation of the functional mechanism of this interesting protein.
Journal ArticleDOI

Lectin Engineering, a Molecular Evolutionary Approach to Expanding the Lectin Utilities

TL;DR: The current state of the art of lectin engineering is summarized and recent technological advances in this field including selection of template lectin, construction of a mutagenesis library, and high-throughput screening methods are discussed.
Book ChapterDOI

Fungal lectins: a growing family.

TL;DR: This chapter provides an overview of the approximately 80 types of mushroom and fungal lectins that have been isolated and studied to date and their properties, sugar-binding specificities, structural grouping into families, and applications for biological research being described.
References
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Journal ArticleDOI

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

TL;DR: A discontinuous sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) system for the separation of proteins in the range from 1 to 100 kDa is described, and the omission of glycine and urea prevents disturbances which might occur in the course of subsequent amino acid sequencing.
Journal ArticleDOI

Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes.

TL;DR: Small amounts of myoglobin, beta-lactoglobulin, and other proteins and peptides can be spotted or electroblotted onto polyvinylidene difluoride membranes, stained with Coomassie Blue, and sequenced directly, suggesting that PVDF membranes are superior supports for sequence analysis of picomole quantities of proteins purified by gel electrophoresis.
Journal ArticleDOI

Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate.

TL;DR: All amino acids, including proline, are converted quantitatively to phenylthiocarbamyl compounds and these are stable enough to eliminate any need for in-line derivatization, providing results comparable in sensitivity and precision to those obtained by state-of-the-art ion-exchange analyzers.
Journal ArticleDOI

The family of metazoan metal-independent β-galactoside-binding lectins: structure, function and molecular evolution

TL;DR: It appears that beta-galactoside-binding lectins and some non-lectin proteins form a superfamily whose members are widely distributed from vertebrates to invertebrates and a consideration of molecular evolution suggests that lectins belonging to this family probably existed in the Precambrian era.
Journal ArticleDOI

Galectins: A Family of Animal Lectins That Decipher Glycocodes

TL;DR: Crystallographic studies revealed that galectins and legume lectins such as concanavalin A have a common topology in spite of the absence of sequence homology, which suggests a possible relationship between animal and plant lectins, and the existence of a lectin super family.
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