Title : Cloning and Characterization of Surface-Localized α-Enolase of Streptococcus iniae, an Effective Protective Antigen in Mice.

Pub. Date : 2015 Jun 25

PMID : 26121302






2 Functional Relationships(s)
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1 The functional identity of the purified recombinant alpha-enolase protein was verified by its ability to catalyze the conversion of 2-phosphoglycerate (2-PGE) to phosphoenolpyruvate (PEP), and both the recombinant and native proteins interacted with human plasminogen. 2-phosphoglycerate enolase 1 Homo sapiens
2 The functional identity of the purified recombinant alpha-enolase protein was verified by its ability to catalyze the conversion of 2-phosphoglycerate (2-PGE) to phosphoenolpyruvate (PEP), and both the recombinant and native proteins interacted with human plasminogen. 2-phosphoglycerate enolase 1 Homo sapiens