Study of different hormone-sensitive lipase concentrations using a surface plasmon resonance sensor

F. Meriaudeau, T. L. Ferrell, E. T. Arakawa, A. Wig, A. Passian, T. Thundat, W. J. Shen, S. Patel, F. B. Kraemer

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

This paper presents a series of experimental results including those based on the surface plasmon resonance (SPR) to investigate the parameters for determining the concentration and form of various hormone sensitive lipase (HSL) solutions. HSL is a rate-limiting enzyme for the metabolism of stored fat. This small protein was not previously known to possess optical properties permitting studies by attenuated total internal reflection (ATR) spectroscopy or by the SPR method. Therefore, basic physical measurements were needed. The HSL solutions are typically contained in different buffers that chemically affect the metal layers in the SPR experiments and cause problems with film integrity. Different experiments employing different metal layers were conducted. The results were compared with those of the ATR method, showing the expected greater sensitivity of the surface plasmon resonance method. It was determined that the protein solutions may be usefully examined by both methods ultimately permitting measurement of oligomer formation as a function of concentration in future work.

Original languageEnglish
Pages (from-to)192-198
Number of pages7
JournalSensors and Actuators, B: Chemical
Volume73
Issue number2-3
DOIs
StatePublished - Mar 10 2001

Funding

Oak Ridge National Laboratory is managed by UT-Battelle, LLC, for the US Department of Energy under contract DE-AC05-00OR22725.

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