Journal ArticleDOI
Agrocybe cylindracea lectin is a member of the galectin family.
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.read more
Citations
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Journal ArticleDOI
Importance of nuclear localization for the apoptosis-induced activity of a fungal galectin AAL (Agrocybe aegerita lectin)
Yi Liang,Lei Feng,Xin Tong,Kun Wang,De-Feng Li,Jia Cheng Lin,Zi Jian Tang,Hong Hong Liu,Shuai Jiang,Lin Guo,Da-Cheng Wang,Hui Sun +11 more
TL;DR: These findings provide a novel antitumor mechanism of fungal galectin by observing AAL to translocate into the HeLa cell nucleus and induce cell apoptosis when it was predominantly in the nucleus.
Journal ArticleDOI
The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A
TL;DR: Evidence suggests that SSA represents a novel family of fungal lectins with a unique sequence and sugar-binding properties and is confined to a small taxonomic group of the Ascomycota.
Proteins expressed during hyphal aggregation for fruiting body formation in basidiomycetes
Kiran Lakkireddy,Mónica Navarro-González,Rajesh Velagapudi,Ursula Kües,J. M. Savoie,M. Foulongne-Oriol,M. Largeteau,Gérard Barroso +7 more
TL;DR: Following up the distribution of genes for proteins with lectin and/or hemolysin function in the steadily growing number of available genomes of basidiomycetes finds an essential role for such functions in hyphal aggregation unlikely.
Journal ArticleDOI
Primary structure and specificity of a new member of galectin family from the Amethyst deceiver mushroom Laccaria amethystina.
TL;DR: A new galectin was characterized in the Amethyst deceiver mushroom Laccaria amethystina and the complete amino acid (AA) sequence of the lectin, which exhibited β-galactoside specificity, was deduced from its peptide sequences.
References
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H. Schägger,G. von Jagow +1 more
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.
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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
Jun Hirabayashi,Ken-ichi Kasai +1 more
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
Ken-ichi Kasai,Jun Hirabayashi +1 more
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.