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Quizzes > Science > Chemistry

Which Additive Prevents Glycolysis? Take the Quiz Now!

Ready to explore glycolysis inhibitor additives and see if you can prevent glycolysis in cells?

Difficulty: Moderate
2-5mins
Learning OutcomesCheat Sheet
Paper art illustration of molecular model and test tubes symbolizing glycolysis inhibitor quiz on golden yellow background

This quiz helps you figure out which additive prevents glycolysis and how it blocks the pathway in cells and lab samples. Work through short questions to practice recall and check any gaps before an exam; if you want a quick refresher first, try our warm-up quiz .

Which additive is commonly used to prevent glycolysis by inhibiting the enzyme enolase?
Iodoacetate
Sodium fluoride
Sodium oxalate
Potassium arsenate
Fluoride ions inhibit enolase by binding at its active site in a magnesium?dependent manner, preventing the conversion of 2?phosphoglycerate to phosphoenolpyruvate. It is widely used in blood collection tubes to halt glycolytic activity and preserve glucose levels. This mechanism makes sodium fluoride a standard glycolysis inhibitor in clinical chemistry.
Fluoride inhibits which step of glycolysis?
Fructose-6-phosphate to fructose-1,6-bisphosphate
Phosphoenolpyruvate to pyruvate
Glucose to glucose-6-phosphate
2-Phosphoglycerate to phosphoenolpyruvate
The conversion of 2-phosphoglycerate to phosphoenolpyruvate is catalyzed by enolase, which is specifically inhibited by fluoride via sequestration of magnesium at the enzyme's active site. Inhibition here prevents all downstream glycolytic flux. Sodium fluoride is therefore chosen to stop glycolysis at this specific reaction.
Arsenate prevents net ATP formation by acting as an analog of which molecule in glycolysis?
NAD+
ATP
Inorganic phosphate (Pi)
ADP
Arsenate mimics inorganic phosphate in the glyceraldehyde-3-phosphate dehydrogenase reaction, forming 1-arseno-3-phosphoglycerate, which hydrolyzes spontaneously instead of producing ATP via phosphoglycerate kinase. This bypass removes the substrate for ATP generation. As a result, net ATP yield drops to zero.
Iodoacetate prevents glycolysis by covalently modifying which amino acid side chain in glyceraldehyde-3-phosphate dehydrogenase?
Lysine amine
Serine hydroxyl
Cysteine thiol
Histidine imidazole
Iodoacetate is an alkylating agent that specifically reacts with the thiol group of the active-site cysteine in glyceraldehyde-3-phosphate dehydrogenase, irreversibly inhibiting its catalytic activity. This stops the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. Thus, glycolysis is blocked at this step.
Which additive is routinely used in blood collection tubes to preserve plasma glucose by halting glycolysis?
Sodium citrate
Sodium fluoride
EDTA
Heparin
Sodium fluoride is added to blood collection tubes as an enolase inhibitor to prevent glycolytic consumption of glucose post-collection. EDTA and heparin serve anticoagulant roles but do not stop glycolysis. Citrate also chelates calcium for anticoagulation but has no direct effect on glycolytic enzymes.
What is the primary mechanism by which fluoride inhibits enolase?
Mimicking phosphoenolpyruvate structure
Formation of a magnesium - fluoride complex at the active site
Covalent modification of a cysteine residue
Chelation of iron in the enzyme
Fluoride combines with the essential magnesium cofactor at the enolase active site, forming a tight magnesium - fluoride complex that inactivates the enzyme. This prevents the dehydration of 2-phosphoglycerate. There is no covalent bond formation with amino acid residues.
Which additive enters the glycolytic pathway as an analog of inorganic phosphate and causes ATP yield loss?
Iodoacetate
Oxalate
Arsenate
Fluoride
Arsenate replaces inorganic phosphate in the reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase, creating 1-arseno-3-phosphoglycerate which bypasses substrate-level phosphorylation. As a result, the ATP that would have been generated by phosphoglycerate kinase is not produced. This mechanism leads to no net ATP gain.
Which amino acid is targeted by alkylating inhibitors like iodoacetamide in glycolytic enzymes?
Proline
Cysteine
Methionine
Tyrosine
Alkylating agents such as iodoacetamide specifically react with the thiol group of cysteine residues in enzyme active sites. This irreversible modification prevents catalytic function of enzymes like glyceraldehyde-3-phosphate dehydrogenase. Other amino acids are much less nucleophilic and are not targeted.
Which reagent is NOT effective at preventing glycolysis in a blood sample?
Sodium fluoride
Potassium oxalate
Sodium iodoacetate
EDTA
EDTA acts as an anticoagulant by chelating calcium ions but does not inhibit any glycolytic enzymes. Sodium fluoride, potassium oxalate, and sodium iodoacetate each prevent glycolysis by inhibiting specific enzymes or chelating essential cofactors. Therefore, EDTA alone will not stop glycolysis.
Which additive directly disrupts the enzyme activity of glyceraldehyde-3-phosphate dehydrogenase?
Sodium fluoride
Iodoacetate
Sodium oxalate
Potassium arsenate
Iodoacetate alkylates the critical cysteine thiol in the active site of glyceraldehyde-3-phosphate dehydrogenase, irreversibly blocking its catalytic function. Fluoride and oxalate inhibit other enzymes, while arsenate bypasses ATP generation without directly modifying the enzyme.
Which additive prevents glycolysis by targeting enolase but requires a divalent cation cofactor?
Fluoride
Iodoacetate
DEPC
Arsenate
Fluoride requires magnesium ions to form a complex at the enolase active site, inactivating the enzyme. Iodoacetate and arsenate act on different targets, and DEPC modifies histidine residues, not specifically enolase.
Which additive is known to cause an apparent loss of inorganic phosphate in glyceraldehyde-3-phosphate dehydrogenase assays?
Sodium citrate
Arsenate
Fluoride
Iodoacetate
Arsenate forms 1-arseno-3-phosphoglycerate, which hydrolyzes spontaneously and releases arsenate instead of phosphate, making it appear as if phosphate is lost. Fluoride and iodoacetate act on enzymes without mimicking phosphate. Citrate is a metabolic regulator but does not mimic phosphate.
Why is sodium fluoride often paired with an anticoagulant such as potassium oxalate in blood collection tubes?
To buffer pH and inhibit enzymes
To prevent both clotting and glycolysis
To chelate iron
To precipitate proteins
Sodium fluoride inhibits glycolysis by targeting enolase, while potassium oxalate chelates calcium to prevent blood clotting. Their combination ensures that blood remains fluid and glucose levels stay constant. Neither is used primarily for buffering or protein precipitation in this context.
Which additive would you choose to irreversibly halt glycolysis at the glyceraldehyde-3-phosphate dehydrogenase step?
Arsenate
Iodoacetate
Fluoride
Sodium oxalate
Iodoacetate irreversibly alkylates the active-site cysteine of glyceraldehyde-3-phosphate dehydrogenase, permanently blocking its activity. Fluoride and oxalate target different steps, and arsenate bypasses ATP formation rather than stopping the enzyme covalently.
How does arsenate decrease the net ATP yield of glycolysis?
Oxidizes NADH directly
Chelates magnesium ions
Inhibits hexokinase
Forms 1-arseno-3-phosphoglycerate which hydrolyzes spontaneously
Arsenate replaces phosphate in the GAPDH reaction to form 1-arseno-3-phosphoglycerate, which hydrolyzes without producing ATP via phosphoglycerate kinase. This bypass prevents formation of ATP at that step, dropping net yield to zero. Arsenate does not inhibit hexokinase, chelate magnesium, or oxidize NADH directly.
Bromopyruvate inhibits glycolysis by alkylating which enzyme?
Aldolase
Phosphoglycerate kinase
Hexokinase
Enolase
Bromopyruvate is a potent alkylating agent that targets and inactivates hexokinase, blocking the phosphorylation of glucose in the first step of glycolysis. It does not affect enolase, phosphoglycerate kinase, or aldolase directly. This specificity makes it a useful tool in metabolic studies.
2-Deoxyglucose acts as an additive to prevent glycolysis by inhibiting which enzyme?
Enolase
Glyceraldehyde-3-phosphate dehydrogenase
Hexokinase
Phosphofructokinase
2-Deoxyglucose is phosphorylated by hexokinase to 2-deoxyglucose-6-phosphate but cannot be further metabolized, thereby inhibiting hexokinase activity by product inhibition and blocking glucose flux through glycolysis. It does not directly inhibit phosphofructokinase, enolase, or GAPDH.
What is the net ATP yield per glucose when arsenate is present throughout glycolysis?
1
2
-1
0
Because arsenate bypasses the phosphoglycerate kinase step by forming 1-arseno-3-phosphoglycerate that hydrolyzes without producing ATP, the two ATP molecules formed by hexokinase and phosphofructokinase are consumed without any offsetting ATP generation, giving a net yield of zero.
What type of inhibition does fluoride exhibit on enolase based on kinetic studies?
Uncompetitive
Noncompetitive
Competitive
Mixed
Fluoride binds to the enzyme - substrate - magnesium complex of enolase, reducing both Vmax and Km in parallel in Lineweaver - Burk plots, a hallmark of uncompetitive inhibition. It does not compete with substrate for the free enzyme, ruling out competitive or noncompetitive mechanisms.
Which additive would you use to specifically inhibit glyceraldehyde-3-phosphate dehydrogenase without affecting hexokinase?
Bromopyruvate
Fluoride
Arsenate
Iodoacetate
Iodoacetate selectively alkylates the active?site cysteine of GAPDH, leaving hexokinase and other early glycolytic enzymes unaffected. Fluoride targets enolase, arsenate bypasses ATP generation, and bromopyruvate attacks hexokinase.
p-Chloromercuribenzoate inhibits glycolytic enzymes by reacting with which functional group?
Phosphate ( - PO4)
Thiol ( - SH)
Amine ( - NH2)
Carboxyl ( - COOH)
p-Chloromercuribenzoate forms mercurial bonds with thiol groups in active?site cysteine residues of proteins, including key glycolytic enzymes like GAPDH, thereby inhibiting their catalytic activity. It does not react specifically with carboxyl, amine, or phosphate groups.
Diethyl pyrocarbonate (DEPC) can inhibit glycolysis by modifying which amino acid residue?
Threonine
Glutamate
Histidine
Proline
DEPC specifically carbethoxylates histidine imidazole rings, blocking their participation in enzyme active sites. Many glycolytic enzymes rely on histidine residues for proton transfers, so DEPC can inhibit their function. It does not target proline, glutamate, or threonine.
Mercuric chloride inhibits glycolysis by binding to which group on enzymes?
Amino groups
Thiol groups
Carboxyl groups
Hydroxyl groups
Mercuric chloride forms strong mercurial bonds with thiol ( - SH) groups in cysteine residues, inactivating thiol?dependent enzymes like GAPDH. It does not selectively bind to hydroxyl, carboxyl, or amino groups with the same affinity.
Which additive would you choose to trap the enediolate intermediate of enolase for structural studies?
DEPC
Arsenate
Fluoride
Iodoacetate
Fluoride forms a stable complex with the enediolate intermediate and magnesium at the enolase active site, facilitating crystallographic trapping of that state. Arsenate bypasses glyceraldehyde-3-phosphate dehydrogenase, and iodoacetate/DEPC modify different residues.
In the presence of iodoacetamide, which glycolytic intermediate is expected to accumulate?
Glucose-6-phosphate
Glyceraldehyde-3-phosphate
Fructose-1,6-bisphosphate
2-Phosphoglycerate
Iodoacetamide inactivates GAPDH, preventing the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. As a result, glyceraldehyde-3-phosphate builds up upstream. Other intermediates downstream or at different steps are not directly affected.
Which additive competes with phosphate and leads to bypassing of the phosphoglycerate kinase reaction?
Fluoride
Arsenate
Iodoacetate
Bromopyruvate
Arsenate mimics phosphate in the GAPDH reaction, forming a labile 1-arseno-3-phosphoglycerate that never becomes substrate for phosphoglycerate kinase, thus bypassing that ATP?generating step. Fluoride inhibits enolase, iodoacetate alkylates GAPDH, and bromopyruvate targets hexokinase.
Which reagent would you use to stop glycolysis immediately in a lysate by inactivating histidine residues?
Sodium fluoride
Sodium oxalate
Potassium arsenate
Diethyl pyrocarbonate (DEPC)
DEPC selectively modifies histidine residues by carbethoxylation, disrupting acid - base catalysts in many glycolytic enzymes including enolase. Fluoride, arsenate, and oxalate act on non-histidine targets. DEPC is the reagent of choice for histidine-specific inactivation.
In a Lineweaver - Burk plot for enolase with fluoride, what pattern indicates uncompetitive inhibition?
Converging above the x-axis
Intersecting at the x-axis
Parallel lines compared to control
Intersecting at the y-axis
Uncompetitive inhibitors bind only to the enzyme - substrate complex, producing parallel lines in Lineweaver - Burk plots with both Vmax and Km decreased equally. Competitive inhibitors intersect at the y-axis, while noncompetitive inhibitors intersect on the x-axis. Parallel lines are diagnostic of uncompetitive inhibition.
Which kinetic parameter(s) change under fluoride inhibition of enolase?
Km increases only
Both Km and Vmax decrease
Vmax decreases only
Km decreases and Vmax increases
As an uncompetitive inhibitor, fluoride lowers both Km and Vmax for enolase in equal proportion. This is because fluoride binds only to the enzyme - substrate - Mg complex, stabilizing it but preventing catalysis. The signature is a reduction of both parameters.
When arsenate is used in glycolytic assays, which analytical artifact may occur?
Apparent phosphate disappearance in assays
Spontaneous ADP formation
Shifted pH of assay buffer
Elevated NADH fluorescence
Arsenate forms 1-arseno-3-phosphoglycerate, which hydrolyzes to 3-phosphoglycerate and arsenate, releasing inorganic phosphate that can be lost or mismeasured. This makes it seem as though phosphate has disappeared. NADH fluorescence and pH shifts are not typical arsenate artifacts.
In an 18O-labeling experiment, what happens to the oxygen label of inorganic phosphate when arsenate substitutes for phosphate?
Label is lost due to rapid hydrolysis
Label shifts to enolase
Label is incorporated into ATP
Label remains on glyceraldehyde-3-phosphate
The 1-arseno-3-phosphoglycerate intermediate hydrolyzes spontaneously, releasing unlabeled arsenate and losing the 18O label on phosphate, so labeled oxygen does not appear in downstream metabolites. No ATP is produced, and glyceraldehyde-3-phosphate is upstream.
Which combination of additives is optimal to prevent glycolysis and clotting in whole blood assays?
Potassium oxalate alone
Iodoacetate plus citrate
Heparin plus arsenate
Sodium fluoride plus EDTA
Sodium fluoride halts glycolysis by inhibiting enolase, while EDTA chelates calcium to prevent clotting. Potassium oxalate also chelates calcium but is often replaced with EDTA for broader metal binding. Heparin does not stop glycolysis, and citrate or arsenate combinations are less standard.
How does pH influence fluoride's ability to inhibit enolase?
Lower pH converts fluoride to HF2 -
pH has no effect
Higher pH converts fluoride to F2 gas
Lower pH increases HF formation and enzyme penetration
At lower pH, more hydrogen fluoride (HF) forms, which can cross membranes and reach intracellular enolase more effectively. Once inside, HF dissociates to F - and H+, inhibiting the enzyme. Pure fluoride activity is affected by pH equilibrium.
Excess free cysteine can reverse inhibition by iodoacetate if added before enzyme exposure. What type of inhibition does this suggest?
Irreversible but competitive for reagent
Reversible competitive
Reversible noncompetitive
Irreversible uncompetitive
Addition of free cysteine can consume iodoacetate before it alkylates enzyme cysteines, preventing inhibition. This shows that inhibition is irreversible once the enzyme is modified, but free cysteine acts as a sacrificial competitor for the reagent.
Which spectroscopic change would you monitor to quantify enolase inhibition by fluoride?
Decrease in absorbance at 240 nm for PEP formation
Increase in NADH fluorescence
Decrease in absorbance at 280 nm
Shift in circular dichroism at 215 nm
Enolase activity is often monitored by the increase in absorbance at 240 nm due to phosphoenolpyruvate formation. Fluoride inhibition reduces PEP production, lowering the 240 nm signal. NADH assays measure GAPDH steps, and 280 nm changes track protein folding, not catalysis.
How would you distinguish competitive from uncompetitive inhibition of enolase by fluoride using Michaelis - Menten kinetics?
Uncompetitive shows parallel Lineweaver - Burk lines
Noncompetitive shows parallel lines
Mixed shows parallel lines
Competitive shows parallel lines
Uncompetitive inhibition yields parallel lines in Lineweaver - Burk plots because both Km and Vmax are reduced proportionally. Competitive inhibition yields lines intersecting at the y-axis, while noncompetitive yields intersection on the x-axis. Mixed inhibition patterns vary.
Which parameter would remain unchanged if fluoride acted as a pure competitive inhibitor of enolase?
Km
kcat/Km
Vmax
Both Vmax and Km
Pure competitive inhibition increases Km without changing Vmax, as high substrate can outcompete the inhibitor. If fluoride were purely competitive, Vmax would stay constant. In reality, fluoride is uncompetitive, affecting both parameters.
Why might arsenate-treated glycolytic reactions show an apparent uptake of inorganic phosphate when measured colorimetrically?
Spontaneous hydrolysis of 1-arseno-3-phosphoglycerate releases arsenate, not Pi, skewing assays
Arsenate increases NADH absorbance
Arsenate forms colored complexes with assay reagent
Arsenate raises pH, altering dye reaction
The labile arsenate ester hydrolyzes rapidly, releasing arsenate rather than phosphate; many colorimetric assays detect free phosphate and register decreased levels, leading to apparent uptake. Arsenate does not produce colored complexes or directly affect NADH absorbance. pH changes are minimal in buffered systems.
Which method can you use to confirm covalent modification of GAPDH by iodoacetate?
Mass spectrometry of the modified enzyme
Thermal shift assay
Size-exclusion chromatography
UV - Vis absorbance at 260 nm
Mass spectrometry can detect the mass increase from alkylation of cysteine residues by iodoacetate, providing direct evidence of covalent modification. UV - Vis at 260 nm monitors nucleic acids, thermal shift measures stability changes, and size-exclusion tracks size, not specific covalent adducts.
In a mixed inhibition scenario of enolase by fluoride, which plot feature would you observe?
Intersect on the x-axis
Lines intersect left of the y-axis
Intersect at the y-axis
Parallel lines
Mixed inhibition yields Lineweaver - Burk lines that intersect left of the y-axis (above or below the x-axis), indicating different effects on Km and Vmax. Uncompetitive gives parallel lines, competitive intersects at y-axis, and noncompetitive at the x-axis.
When designing a high-throughput assay to screen for new glycolysis inhibitors, which additive would you include as a positive control for enolase inhibition?
Sodium fluoride
Bromopyruvate
Potassium arsenate
Iodoacetamide
Sodium fluoride is well?characterized as an enolase inhibitor and provides a robust positive control to benchmark new compounds. Iodoacetamide targets GAPDH, arsenate bypasses ATP formation, and bromopyruvate attacks hexokinase. Using NaF ensures assay specificity for the enolase step.
In a computational docking study, which residue would you target to model iodoacetate binding to GAPDH?
Histidine-179
Serine-151
Lysine-184
Cysteine-149
Cysteine-149 in GAPDH is the active-site nucleophile that reacts with iodoacetate, forming a covalent adduct. Histidine-179 participates in catalysis but is not alkylated by iodoacetate. Lysine and serine residues are not primary targets for this reagent.
Which structural feature of arsenate accounts for its rapid hydrolysis compared to phosphate esters in enzymatic reactions?
Stronger hydrogen bonding
Extra negative charge
Longer As - O bonds and lower tetrahedral stability
Higher pKa of conjugate acid
Arsenate esters are less stable than phosphate esters because the As - O bond is longer and the tetrahedral intermediate is less favorable, leading to spontaneous hydrolysis. The charge difference and pKa values are similar, and hydrogen bonding does not dominate this effect.
In engineering an enolase variant resistant to fluoride, which active-site mutation would most likely reduce fluoride binding without abolishing catalysis?
Replace histidine with proline
Replace a coordinating serine with alanine
Replace lysine with arginine
Replace active-site cysteine with serine
Fluoride inhibition relies on interaction with active-site residues coordinating magnesium, including serine. Mutating a coordinating serine to alanine can reduce fluoride binding while retaining catalytic metals. Cysteine, histidine, or lysine mutations would disrupt the mechanism more severely.
Which isotope-labeling strategy would you use to distinguish phosphate incorporation from arsenate labeling in glycolytic intermediates?
Use 13C-labeled glucose
Use 32P and autoradiography
Use 18O-labeled water
Use 33P-labeled phosphate and monitor by NMR
33P is a stable NMR-active isotope that can be distinguished from arsenic signals in 31P NMR, allowing direct monitoring of phosphate incorporation versus arsenate. 32P autoradiography cannot differentiate arsenate, 18O labels water, and 13C tracks carbon atoms.
If you wanted to design an inhibitor that mimics the transition state of the enolase reaction, which functional groups would you incorporate?
Michael acceptor
Aromatic sulfonate
Aliphatic phosphate analog
Fluorinated ?-hydroxycarboxylate with metal-chelating moiety
Enolase's transition state involves a ?-hydroxycarboxylate anion stabilized by magnesium; a fluorinated analog with a strong metal-chelating group would best mimic that state. Aromatic sulfonates or phosphate analogs do not recapitulate the hydroxycarboxylate geometry, and Michael acceptors target different enzyme classes.
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Study Outcomes

  1. Identify Additives that Prevent Glycolysis -

    Recognize common compounds used to prevent glycolysis, such as fluoride or iodoacetate, and understand their relevance in lab settings and biochemistry quizzes.

  2. Explain Mechanisms of Glycolysis Inhibitor Additives -

    Describe how different glycolysis inhibitor additives interact with specific enzymes to block metabolic pathways and halt ATP production.

  3. Analyze Biochemistry Quiz Scenarios -

    Interpret quiz questions on glycolysis questions to determine which additive inhibits glycolysis under various experimental conditions.

  4. Apply Knowledge to Prevent Glycolysis in Cells -

    Use your understanding of additive choices to design experiments that effectively prevent glycolysis in cells for research purposes.

  5. Evaluate Impact of Inhibitors on Cellular Metabolism -

    Assess how different additives that inhibit glycolysis affect downstream metabolic pathways and overall cell physiology.

  6. Recall Key Enzymatic Targets of Common Additives -

    Memorize which glycolytic enzymes are targeted by specific inhibitors, enhancing your ability to answer related quiz questions accurately.

Cheat Sheet

  1. Fluoride's Enolase Inhibition -

    When asking which additive prevents glycolysis, sodium fluoride (NaF) deserves first mention as a glycolysis inhibitor additive targeting enolase to block 2-phosphoglycerate conversion to phosphoenolpyruvate. By chelating Mg2+ at the active site, it effectively prevents glycolysis in cells within blood samples, preserving metabolite levels. Remember "F → Freeze" to recall how fluoride freezes glycolytic flux (University of Oxford Biochemical Methods).

  2. Iodoacetate and GAPDH Covalent Modification -

    Iodoacetate alkylates the catalytic cysteine of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), halting the oxidative phosphorylation of glyceraldehyde-3-phosphate. This additive that inhibits glycolysis proves invaluable in lab assays by irreversibly deactivating a key enzyme early in the pathway. Mnemonic tip: "Iodine Attaches" to remember how iodoacetate attaches to GAPDH (Voet & Voet, Biochemistry).

  3. Arsenate as a Phosphate Analog -

    Arsenate acts as a glycolysis inhibitor additive by mimicking inorganic phosphate, forming 1-arseno-3-phosphoglycerate that rapidly hydrolyzes without ATP production. This "arsenate bypass" leaves glycolysis energetically futile, so no net ATP is gained in that step. Think "As = As_gonic" to recall arsenate disrupts the energy harvest (J. Biol. Chem., 2002).

  4. 2-Deoxyglucose Glucose-6-Phosphate Trap -

    2-Deoxyglucose (2-DG) is a glucose analog used in biochemistry quizzes and experiments to prevent glycolysis in cells by competitively inhibiting hexokinase and trapping 2-DG-6-P. Since 2-DG-6-P cannot be further metabolized, it accumulates and stalls the pathway at step 1. Use the "2-DG Trap" when designing glycolysis questions or metabolic flux analyses (Science, 1992).

  5. Sample Preservation: NaF and EDTA Combo -

    In clinical biochemistry, adding sodium fluoride with EDTA to blood collection tubes is a proven strategy to block glycolysis, ensuring stable glucose readings. NaF inhibits enolase while EDTA chelates Mg2+, synergistically preventing metabolic breakdown of glucose. This combo is known as the gold standard for "prevent glycolysis in cells" protocols (CDC Guidelines, 2020).

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