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Rate of dissociation of PLP from the ePL kinase•PLP complex.

By Mohini S. Ghatge (314266), Roberto Contestabile (314268), Martino L. di Salvo (314273), Jigar V. Desai (183106), Amit K. Gandhi (314278), Christina M. Camara (314282), Rita Florio (314284), Isabel N. González (314285), Alessia Parroni (314286), Verne Schirch (314287) and Martin K. Safo (314288)

Abstract

<p>The rate of dissociation of PLP from the <i>e</i>PL kinase•PLP complex was followed by observing the change in optical activity of the bound PLP at 37°C. Panel A: Spectra of the complex (60 µM) at time zero (curve a) and after 120 min in the presence of 10 µM PLP phosphatase (curve b). Panel B: measured decrease in optical activity after addition of PLP phosphatase at 415 nm with time and as an exponential process with rate constant of 0.012 min<sup>−1</sup>.</p

Topics: Biochemistry, Physics, Biological Sciences, dissociation, plp, epl
Year: 2013
DOI identifier: 10.1371/journal.pone.0041680.g005
OAI identifier: oai:figshare.com:article/273847
Provided by: FigShare
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