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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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine heart

Quality Level

form

ammonium sulfate suspension

specific activity

≥200 units/mg protein

UniProt accession no.

foreign activity

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

storage temp.

2-8°C

Gene Information

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

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Clinical Biochemistry and Hematology
Washington IM and Hoosier GV
Journal of Separation Science, 57-116 (2012)
Biochemistry, Lactate Dehydrogenase
Farhana A and Lappin SL
StatPearls [Internet] (2023)
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
J A Read et al.
Proteins, 43(2), 175-185 (2001-03-29)
Lactate dehydrogenase (LDH) interconverts pyruvate and lactate with concomitant interconversion of NADH and NAD(+). Although crystal structures of a variety of LDH have previously been described, a notable absence has been any of the three known human forms of this
Minh Vu Chuong Nguyen et al.
Biochemical pharmacology, 85(11), 1644-1654 (2013-04-16)
NADPH oxidase Nox4 is expressed in a wide range of tissues and plays a role in cellular signaling by providing reactive oxygen species (ROS) as intracellular messengers. Nox4 oxidase activity is thought to be constitutive and regulated at the transcriptional

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

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

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