当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Purification and characterization of a heterodimeric mycelial lectin from Penicillium proteolyticum with potent mitogenic activity.

Purification and characterization of a heterodimeric mycelial lectin from Penicillium proteolyticum with potent mitogenic activity.

Abstract：

:In the present study, Penicillium proteolyticum lectin was purified by DEAE-Sepharose chromatography followed by Sephadex G-100 gel filtration chromatography. A sequence of ion-exchange and gel filtration chromatography resulted in 52.30 fold purified lectin with a high yield of 84.21%. The purified P. proteolyticum lectin is a glycoprotein with 2.83% linked carbohydrates. A single band in Native-PAGE, whereas two bands (25.1 kDa and 22.9 kDa) in SDS-PAGE confirmed the heterodimeric nature of the purified lectin. The apparent molecular weight (48 kDa) of P. proteolyticum lectin was further confirmed by gel filtration analysis. Heterodimeric P. proteolyticum lectin was stable within a pH range of 6.5-7.5 and upto a temperature of 30 °C. The lectin activity was strongly inhibited by complex glycoproteins and denaturants. Metal ions are not required for agglutination activity of purified lectin. The lectin showed significant mitogenic response towards mice splenocytes. It exhibited highest mitogenic activity at a concentration of 50 μg/mL. This is a first report on characteristics of purified P. proteolyticum lectin having potent mitogenic potential.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Singh RS,Walia AK,Kennedy JF

doi

10.1016/j.ijbiomac.2019.01.103

subject

Has Abstract

pub_date

2019-05-01 00:00:00

pages

124-131

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)30035-2

journal_volume

128

pub_type

杂志文章

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