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L7525

Sigma-Aldrich

L-Lactic Dehydrogenase from porcine heart

ammonium sulfate suspension, ≥200 units/mg protein

Synonym(s):

(S)-Lactate: NAD+ oxidoreductase, L-LDH, LAD, LD, Lactate

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About This Item

CAS Number:
9001-60-9
Enzyme Commission number:
1.1.1.27 (BRENDA, IUBMB)
EC Number:
232-617-8
MDL number:
MFCD00131466
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine heart

form

ammonium sulfate suspension

specific activity

≥200 units/mg protein

UniProt accession no.

P00339

foreign activity

glutamic-oxalacetic transaminase ≤0.1%
malic dehydrogenase, glutamic-pyruvic transaminase and pyruvate kinase ≤0.06%

storage temp.

2-8°C

Gene Information

pig ... LDHA(407245)

General description

Research area: Cell Signaling

Lactic Dehydrogenase (LDH) is a cytoplasmic enzyme encoded by LDHA, LDHB, LDHC, and LDHD genes, and categorized as an oxidoreductase. It is widely distributed throughout the body, particularly in muscle, liver, and kidney. LDH demonstrates five isomeric forms that form tetramers with two types of subunits: muscle (M) and heart (H).

application

L-Lactic Dehydrogenase from porcine heart has been used:
  • as a component of the reaction buffer to measure the GTPase activity of EngA bound to the bacterial 50S subunit to study its structure and function.
  • as a component of the enzyme solutions to test the sensitivity of multiphoton NAD(P)H fluorescence lifetime imaging (FLIM) in key enzymatic steps controlling the path of carbon from glucose uptake to electron transport chain (ETC) activity.

Biochem/physiol Actions

Lactate dehydrogenase (LDH) enzyme is responsible for the conversion of pyruvate to lactate, during glycolysis under hypoxic conditions, while also converting NADH to NAD+. Moreover it acts as a crucial regulator of gluconeogenesis and DNA metabolism. Increased serum LDH levels are detected in conditions such as cancer, HIV infection, muscular dystrophy, megaloblastic anemia, extreme hypothermia, hepatitis, meningitis, hypoxia, etc.
Also catalyzes the oxidation of other L-2-hydroxymonocarboxylic acids.

Unit Definition

One unit will reduce 1.0 μmole of pyruvate to L-lactate per min at pH 7.5 at 37 °C.

Physical form

Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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Biochemistry, Lactate Dehydrogenase
Farhana A and Lappin SL
StatPearls [Internet] (2023)
Clinical Biochemistry and Hematology
Washington IM and Hoosier GV
Journal of Separation Science, 57-116 (2012)
Joe T Sharick et al.
Scientific reports, 8(1), 5456-5456 (2018-04-05)
While NAD(P)H fluorescence lifetime imaging (FLIM) can detect changes in flux through the TCA cycle and electron transport chain (ETC), it remains unclear whether NAD(P)H FLIM is sensitive to other potential fates of glucose. Glucose carbon can be diverted from
M J Adams et al.
Proceedings of the National Academy of Sciences of the United States of America, 70(7), 1968-1972 (1973-07-01)
The binding of coenzyme and substrate are considered in relation to the known primary and tertiary structure of lactate dehydrogenase (EC 1.1.1.27). The adenine binds in a hydrophobic crevice, and the two coenzyme phosphates are oriented by interactions with the
H P Schär et al.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie, 360(7), 795-807 (1979-07-01)
Lactate dehydrogenases from thermophilic bacilli (Bacillus stearothermophilus, Bacillus caldotenax) and from mesophilic bacilli (Bacillus X1, Bacillus subtilis) have been isolated by a two-step purification procedure. Only one type (LDH-P4) composed of four identical subunits (Mr 34 000 or 36 000)
View All Related Papers

Articles

How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

Enzymatic Assay of L-Lactic Dehydrogenase (EC 1.1.1.27)

This procedure applies to all products from heart muscle that have a specification for L-Lactic Dehydrogenase activity.

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