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IJBT Vol.07(3) [July 2008] >


Title: Amplification, cloning and sequencing of Enterococcus feacalis enolase gene
Authors: Shivaraj, A
Madhusudan, S
Kumar, C Ashok
Isloor, S
Gowda, Veere
Dechamma, H J
Reddy, G R
Suryanarayana, V V S
Keywords: Enolase
Enterococcus feacalis
Cloning vector
Sequence
Nucleotide
Issue Date: Jul-2008
Publisher: CSIR
Abstract: α-Enolase, a key glycolytic enzyme, belongs to a novel class of surface proteins, which do not possess classical machinery for surface transport and transported on the cell surface through an unknown mechanism. It is a multifunctional protein and its ability to serve as a plasminogen receptor on the surface of a variety of hematopoetic, epithelial and endothelial cells suggest that it may play an important role in the intravascular and pericellular fibrinolytic system. Authors have amplified and cloned α-enolase gene of Enterococcus feacalis in a prokaryotic cloning vector, and then transferred it into Escherichia coli. The recombinant enolase vector (r-pBEnol) was isolated and sequenced. The sequence of the cloned enolase from E. feacalis was found identical to that of the E. feacalis V583. The sequence was submitted to NCBI nucleotide data bank and accession number (AM279410) was obtained.
Page(s): 307-312
ISSN: 0972-5849
Source: IJBT Vol.07(3) [July 2008]

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