当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Cloning, expression and characterization of a mucin-binding GAPDH from Lactobacillus acidophilus.

Cloning, expression and characterization of a mucin-binding GAPDH from Lactobacillus acidophilus.

Abstract：

:Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in glycolysis. It is also referred to as a moonlighting protein as it has many diverse functions like regulation of apoptosis, iron homeostasis, cell-matrix interactions, adherence to human colon etc. apart from its principal role in glycolysis. Lactobacilli are lactic acid bacteria which colonize the human gut and confer various health benefits to humans. In the present study, we have cloned, expressed and purified the GAPDH from Lactobacillus acidophilus to get a recombinant product (r-LaGAPDH) and characterized it. Size exclusion chromatography shows that r-LaGAPDH exists as a tetramer in solution and have a mucin binding and hemagglutination activity indicating carbohydrate like binding adhesion mechanism. Fluorescence spectroscopy studies showed an interaction of r-LaGAPDH with mannose, galactose, N-acetylgalactosamine and N-acetylglucosamine with a Kd of 3.6±0.7×10(-3)M, 4.34±0.09×10(-3)M, 4±0.87×10(-3)M and 3.7±0.28×10(-3)M respectively. We hope that this preliminary data will generate more interest in further elucidation of the roles of GAPDH in the adhesion processes of the bacteria.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Patel DK,Shah KR,Pappachan A,Gupta S,Singh DD

doi

10.1016/j.ijbiomac.2016.04.041

subject

Has Abstract

pub_date

2016-10-01 00:00:00

pages

338-46

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(16)30349-X

journal_volume

91

pub_type

杂志文章

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