Rabbit muscle pyruvate kinase

Manufactured by Merck Group

Sourced in United States

Rabbit muscle pyruvate kinase is an enzyme that catalyzes the transfer of a phosphate group from phosphoenolpyruvate to ADP, thereby producing ATP and pyruvate. This enzyme plays a crucial role in the glycolytic pathway, which is the metabolic process that converts glucose into energy for the cell.

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Pyruvate (358 citations) Pyruvate kinase (149 citations) Pyruvate kinase from rabbit muscle (13 citations)

2 protocols using rabbit muscle pyruvate kinase

Characterizing Enzyme Kinetics using Spectrophotometry

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Sucrose, Trizma base, Folin–Ciocalteu phenol reagent, ethyleneglycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid (EGTA), ethylenediaminetetraacetic acid disodium salt dihydrate (EDTA), deoxycholic acid, trehalose, adenosine triphosphate (ATP), fluorescein isothiocyanate (FITC) and rabbit muscle pyruvate kinase were purchased from Sigma-Aldrich Corp. (St. Louis, MO, USA). Rabbit muscle lactate dehydrogenase was purchased from Roche (Basel, Switzerland). Phosphoenolpyruvate (PEP) and nicotinamide adenine dinucleotide (reduced) salt (NADH) were purchased from Chem-Impex International Inc. (Wood Dale, IL, USA). All other reagents were of the highest quality commercially available.

Rivera-Morán M.A, & Sampedro J.G. (2023). Isolation of the Sarcoplasmic Reticulum Ca2+-ATPase from Rabbit Fast-Twitch Muscle. Methods and Protocols, 6(5), 102.

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Purification and Preparation of Protein Complexes

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Ammonium acetate and lyophilized powders of yeast alcohol dehydrogenase and rabbit muscle pyruvate kinase were purchased from Sigma-Aldrich (St. Louis, MO). Wild type and double mutant (E87C, C312T) AmtB protein complex from E. coli was expressed and purified as previously described.^{15 (link)} The GroEL chaperonin complex was purified as previously described.^{16 (link)} More detailed information for these complexes is provided in Supplemental Table S1. All buffers and lyophilized protein samples were dissolved in 18.2 MΩ·cm water (Barnstead Easy Pure II, Thermo Scientific). All samples were buffer exchanged to 200 mM aqueous Ammonium acetate using Micro BioSpin P-6 gel columns (BioRad) at working concentrations of 1–10 μM. For AmtB, the samples were buffer exchanged into 200 mM Ammonium acetate supplemented with 2x critical micelle concentration of tetraethylene glycol monooctyl ether (0.5% C₈E₄).

Mallis C.S., Zheng X., Qiu X., McCabe J.W., Shirzadeh M., Lyu J., Laganowsky A, & Russell D.H. (2020). Development of Native MS Capabilities on an Extended Mass Range Q-TOF MS. International journal of mass spectrometry, 458, 116451.

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