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Purification of a potent mitogenic homodimeric Penicillium griseoroseum lectin and its characterisation
Author(s) -
Singh Ram S.,
Walia Amandeep K.
Publication year - 2019
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201900428
Subject(s) - lectin , molecular mass , concanavalin a , biochemistry , hemagglutination , chemistry , mannose , sephadex , affinity chromatography , sepharose , glucosamine , glycoprotein , microbiology and biotechnology , biology , in vitro , antibody , enzyme , immunology
Abstract Penicillium griseoroseum lectin was 80‐fold purified by successive DEAE Sepharose anion exchange and Sephadex G‐100 gel permeation chromatography. P. griseoroseum lectin exhibited haemagglutination activity towards protease‐treated rabbit erythrocytes. It showed specificity towards various carbohydrates such as d ‐mannose, N ‐acetyl‐ d ‐glucosamine, mucins, and so forth. P. griseoroseum lectin was found as a glycoprotein with glycan content of 4.33%. Purified P. griseoroseum lectin is homodimeric having a molecular mass of 57 kDa with subunit molecular mass of 28.6 kDa. Haemagglutination activity of purified P. griseoroseum lectin was completely stable from 25°C to 35°C at a pH range of 6–7.5. Lectin activity was not influenced by divalent metal ions and denaturants. P. griseoroseum lectin manifested mitogenicity towards mice splenocytes and activity reached a peak at 75 μg/ml of lectin concentration. P. griseoroseum lectin in microgram concentrations stimulated proliferation of mice splenocytes. Thus, P. griseoroseum lectin exhibits potential mitogenicity, which can be exploited for further biomedical applications.