68387-0

Lactate dehydrogenase [Enzymatic activity/volume] in Peritoneal fluid by Lactate to pyruvate reaction

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Part Descriptions

LP15033-1   Lactate dehydrogenase
Lactate dehydrogenase (LDH) is an enzyme (EC 1.1.1.27) present in a wide variety of organisms, including plants and animals. It catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. As it can also catalyze the oxidation of hydroxybutyrate, it is occasionally called hydroxybutyrate dehydrogenase (HBD). Copyright Text is available under the Creative Commons Attribution/Share-Alike License. See http://creativecommons.org/licenses/by-sa/3.0/ for details. Source: Wikipedia, D-lactate (Wikipedia)

LP15033-1   Lactate dehydrogenase
Lactate dehydrogenase (LDH, or also called LD) is an oxidoreductase (LD: EC 1.1.1.27) and is the most important clinically of several dehydrogenases occurring in human serum. LDH catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD. When disease, injury, or toxic material damages tissues, cells release LDH into the bloodstream. Since LDH is a fairly stable enzyme, it has been widely used to evaluate the presence of damage and toxicity of tissue and cells. LDH is cytoplasmic in its cellular location and in any one tissue is composed of one or two of five possible isoenzymes. While many of its clinical applications involve quantification of one or more specific serum isoenzymes, an estimate of total LDH is usually required. Lactate dehydrogenase catalyzes the reversible reaction: L-lactate + NAD <--> pyruvate + NADH. Testing methods either measure the increase in NADH produced in the lactate-to-pyruvate reaction or the decrease in NADH produced in the pyruvate-to-lactate reaction. PMID: 3882046. Reference ranges are highly method dependent. The pyruvate-to-lactate reaction is preferred theoretically because the equilibrium constant is large and the rate for any amount of enzyme is 2-3 times faster, thus smaller sample and shorter observation periods are needed. Disadvantages of the pyruvate-to-lactate reaction are loss of linearity as compared with the lactate-to-pyruvate reaction, and greater substrate inhibition of the enzyme. [Tietz Fourth Edition] Source: Regenstrief LOINC

Reference Information

Fully-Specified Name

Component

Lactate dehydrogenase

Property

CCnc

Time

Pt

System

Periton fld

Scale

Qn

Method

Reaction: lactate to pyruvate

Additional Names

Short Name

LDH Prt L to P-cCnc

Display Name

LDH Lactate to pyruvate reaction (Periton fld) [Catalytic activity/Vol]

Consumer Name Alpha Get Info

Lactate Dehydrogenase (LDH), Peritoneal fluid

Basic Attributes

Class

CHEM

Type

Laboratory

First Released

Version 2.38

Last Updated

Version 2.73

Order vs. Observation

Both

Common Test Rank Get Info

17589

Language Variants Get Info

Related Names

• 2-Hydroxypropanoic acid
• 2-hydroxy-propionate
• 2-hydroxy-propionic acid
• Ascites
• Ascitic fluid
• Ascitis
• Catalytic Concentration
• Chemistry
• Dehydrog
• Dehyrdogenase
• L to P
• L.D.H
• Lact
• Lactic acid
• Lactic acid dehydrogenase
• LD
• LDH
• L-lactate
• L-lactate dehydrogenase
• Peritoneal fluid
• Point in time
• Prt
• QNT
• Quan
• Quant
• Quantitative
• Random
• React
• Rxn
• Tumor marker

Example Units

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CodeSystem lookup

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LOINC Copyright

Copyright © 2024 Regenstrief Institute, Inc. All Rights Reserved. To the extent included herein, the LOINC table and LOINC codes are copyright © 1995-2024, Regenstrief Institute, Inc. and the Logical Observation Identifiers Names and Codes (LOINC) Committee. See https://loinc.org/license for the full LOINC copyright and license.