MétaCan
Menu
← Back to cohort

Development of an Online LC‐MS/MS Method for the Investigation of Enzyme Kinetics Using Trypsinization of Apomyoglobin Protein as a Model System

2021· article· en· W3172508745 on OpenAlexafffund
David A. Barnett, EmmaRae L. Murphy, Andrew P. Joy, Rodney J. Ouellette

Bibliographic record

VenueThe FASEB Journal · 2021
Typearticle
Languageen
FieldChemistry
TopicMass Spectrometry Techniques and Applications
Canadian institutionsAtlantic Cancer Research Institute
FundersAtlantic Canada Opportunities Agency
KeywordsChemistryChromatographyMass spectrometrySelected reaction monitoringTandem mass spectrometryTrypsinizationIonic strengthAnalytical Chemistry (journal)TrypsinEnzymeAqueous solutionOrganic chemistry

Abstract

fetched live from OpenAlex

The optimization of enzymatic protein cleavage by trypsin is often performed “in the dark” wherein researchers perform the reaction under different conditions on a laboratory bench for a single or a small selection of time points. Upon quenching of the trypsinization reaction with a strong acid, the resulting protein reaction mixture is injected onto a liquid chromatography column for profiling of the peptide mixture. The arbitrary selection of enzyme reaction time presents a major limitation to this experimental approach. Herein, we present a “real time” optimization of the enzymatic reaction enabled by performing the reaction within a vial in an autosampler with regular sampling of the mixture. Using this method, we are able to simultaneously monitor degradation of the intact protein target and the release of its tryptic peptides. Peptides with missed cleavage sites may appear and then disappear with time as fully tryptic peptides dominate the endpoint of the reaction. The method can be multiplexed in that we can sample many parallel mixtures in series. This allows us to directly compare such variables as pH, solvent, ionic strength, protein to enzyme ratio, enzyme concentration and metal salts on digestion efficiency while always including a positive control for reference. Our liquid chromatograph‐tandem mass spectrometry analysis platform uses a Dionex Ultimate 3000 interfaced with a hybrid quadrupole‐Orbitrap (Q‐Exactive) mass spectrometer capable of mass resolution of 140,000 and a mass accuracy better than 10 ppm. We are able to monitor the efficiency and kinetics of tryptic digestion of apomyoglobin with high resolution in the time dimension. At room temperature, the enzymatic reaction can take in excess of 12 hours to reach completion compared with about 3 hours at 38 o C. A low percentage of ethanol (~ 0.1%) added to the reaction mixture was shown to double the yield of most peptides while the addition of alkaline earth metals also had beneficial effects, in particular 10 mM barium chloride. Other metals were shown to either inhibit the degradation of apomyoglobin (zinc) or to prevent the detection of the resulting peptides (lead). Overall, the effects of adding barium in the presence of 0.1% ethanol improved peptide yield as much as 11‐fold for the LFTGHPETLEK peptide of apomyoglobin while showing no effect on the tryptic release of the YLEFISDAIIHVLHSK peptide. This method offers a promising strategy for the optimization of targeted protein quantitation as well as a means to study the kinetics and characterize the specificity of other proteolytic enzymes.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.001
metaresearch head score (Gemma)0.001
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Methods · Consensus signal: Methods
Teacher disagreement score0.001
Threshold uncertainty score0.008

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0010.001
Meta-epidemiology (narrow)0.0010.001
Meta-epidemiology (broad)0.0010.001
Bibliometrics0.0010.001
Science and technology studies0.0010.000
Scholarly communication0.0010.001
Open science0.0010.001
Research integrity0.0010.002
Insufficient payload (model declined to judge)0.0010.001

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.059
GPT teacher head0.314
Teacher spread0.255 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreMethods

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2021
Admission routes2
Has abstractyes

Explore more

Same venueThe FASEB Journal→Same topicMass Spectrometry Techniques and Applications→French-language works237,207→