L7525
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
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biological source
Porcine heart
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
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).
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
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)
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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
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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)
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
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Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Protocols
Enzymatic Assay of L-Lactic Dehydrogenase (EC 1.1.1.27)
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