High Throughput Phosphoglycolate Phosphatase Activity Assay Using Crude Leaf Extract and Recombinant Enzyme to Determine Kinetic Parameters K

Ludmila V Roze, Audrey Johnson, Luke M Gregory, Mauricio Tejera-Nieves, Berkley J Walker

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Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

5 authors.

Ludmila V RozeDepartment of Energy - Plant Research Laboratory, Michigan State University, East Lansing, MI, USA.

Audrey JohnsonDepartment of Energy - Plant Research Laboratory, Michigan State University, East Lansing, MI, USA.

Luke M GregoryDepartment of Plant Biology, Michigan State University, East Lansing, MI, USA.

Mauricio Tejera-NievesDepartment of Energy - Plant Research Laboratory, Michigan State University, East Lansing, MI, USA.

Berkley J WalkerDepartment of Energy - Plant Research Laboratory, Michigan State University, East Lansing, MI, USA. Berkley@msu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Determining enzyme activities involved in photorespiration, either in a crude plant tissue extract or in a preparation of a recombinant enzyme, is time-consuming, especially when large number of samples need to be processed. This chapter presents a phosphoglycolate phosphatase (PGLP) activity assay that is adapted for use in a 96-well microplate format. The microplate format for the assay requires fewer enzymes and reagents and allows rapid and less expensive measurement of PGLP enzyme activity. The small volume of reaction mix in a 96-well microplate format enables the determination of PGLP enzyme activity for screening many plant samples, multiple enzyme activities using the same protein extract, and/or identifying kinetic parameters for a recombinant enzyme. To assist in preparing assay reagents, we also present an R Shiny buffer preparation app for PGLP and other photorespiratory enzyme activities and a K

Indexed as

Enzyme AssaysPhosphoric Monoester HydrolasesPlant ExtractsPlant LeavesRecombinant ProteinsHigh-Throughput Screening AssaysKineticsphosphoglycolate phosphatasePhosphoric Monoester HydrolasesPlant ExtractsRecombinant ProteinsBuffer preparation appKm and Vmax calculation appMentenMichaelisPhosphoglycolate phosphatasePhotorespirationRecombinant phosphoglycolate phosphatase

Identifiers

PMID38861074

DOI10.1016/S0003-2670(00)85116-8

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.