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Role of lysines in enolase/plasminogen binding activity.

By Angela M. Floden (334789), John A. Watt (340107) and Catherine A. Brissette (36177)

Abstract

<p>Binding of plasminogen to immobilized enolase (10 µg/ml) was analyzed by ELISA. Plasminogen (25 µg/ml) was added to enolase-coated wells in the presence or absence of 0–30 mM ε-aminocaproic acid (lysine analog). Bound plasminogen was detected using a specific antiserum. BSA was used as a negative control. Data represent the means and standard errors from three separate experiments with 12 replicates per condition. ***, <i>P</i><0.001, Student's <i>t</i> test assuming unequal variances.</p

Topics: Biochemistry, Microbiology, Infectious Diseases, lysines, binding
Year: 2013
DOI identifier: 10.1371/journal.pone.0027502.g005
OAI identifier: oai:figshare.com:article/385944
Provided by: FigShare
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