Physicochemical properties of micromycetes Alternaria alternate 4 lectin

The physicochemical properties of the lectin of the lower fungus, micromycetes Alternaria alternate 4 have been studied. It was found that the lectin of the micromycetes Alternaria alternate 4 is stable over a wide range of temperatures and pH values (5-70oC and pH 6.0-9.0). The greatest activity of lectin was observed at a temperature of 5-50 °C and a pH of 6.5-8.5. The increased activity of Alternaria alternate 4 lectin was facilitated by the presence of divalent Ca2+, Mn2+, and Zn2+ ions in the reaction mixture, which indicates that Alternaria alternate 4 lectin is a metal-dependent glycoprotein. Alternaria alternate 4 lectin had the ability to bind simple carbohydrates. The activity of Alternaria alternate 4 lectin was inhibited to a greater extent by galactose, which indicates that Alternaria alternate 4 lectin belongs to the group of galactose-binding lectins.

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Publication Details

Journal
Zenodo (CERN European Organization for Nuclear Research)
Published
2025-06-30
DOI
https://doi.org/10.5281/zenodo.17198006
Primary Topic
Diverse Scientific and Economic Studies
Type
article
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article

Physicochemical properties of micromycetes Alternaria alternate 4 lectin

Zenodo (CERN European Organization for Nuclear Research)
Diverse Scientific and Economic Studies
article

Physicochemical properties of micromycetes Alternaria alternate 4 lectin

article en

Abstract

The physicochemical properties of the lectin of the lower fungus, micromycetes Alternaria alternate 4 have been studied. It was found that the lectin of the micromycetes Alternaria alternate 4 is stable over a wide range of temperatures and pH values (5-70oC and pH 6.0-9.0). The greatest activity of lectin was observed at a temperature of 5-50 °C and a pH of 6.5-8.5. The increased activity of Alternaria alternate 4 lectin was facilitated by the presence of divalent Ca2+, Mn2+, and Zn2+ ions in the reaction mixture, which indicates that Alternaria alternate 4 lectin is a metal-dependent glycoprotein. Alternaria alternate 4 lectin had the ability to bind simple carbohydrates. The activity of Alternaria alternate 4 lectin was inhibited to a greater extent by galactose, which indicates that Alternaria alternate 4 lectin belongs to the group of galactose-binding lectins.

Zenodo (CERN European Organization for Nuclear Research)
Kazan Federal University (RU)
Openalex Percentile: Top 35%
Diverse Scientific and Economic Studies
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