34402-8

Coproporphyrin/Hemoglobin [Mass Ratio] in Red Blood Cells

Active

Part Descriptions

LP15151-1   Coproporphyrin
4 carboxyl groups Source: Regenstrief Institute

LP15151-1   Coproporphyrin
Porphyrins build up among patients with hereditary enzyme disorders known as porphyrias. Porphyrias affect the heme biosynthetic pathway and cause increased urine excretion of porphyrinogens, by-products known as porphyrins and porphyrinogen precursors-including delta aminolevulinic acid (ALA) and porphobilinogen (PBG). Coproporphyrin and uroporphyrin excretion in urine is markedly increased during acute attacks of hereditary coproporphyria. Increased uroporphyrinogen, uroporphyrin, and coproporphyrin excretion occurs in porphyria cutanea tarda. Increased coproporphyrin excretion alone lacks specificity and sensitivity for lead testing and is likely to occur secondary to other diseases. Information from LOINC partner 1 and Jacobs and DeMott Laboratory Test Handbook, 5th edition, DS Jacobs, WR DeMott and DK Oxley, 2001. 2007 08 06. Source: Regenstrief Institute

LP15151-1   Coproporphyrin
Part of porphyrin fractionation testing useful in diagnosing porphyrin cutanea tarda, hereditary coproporphyria, and variegate porphyria. Such patients typically will present with profound elevations of porphyrin analytes (e.g. > 5-fold) during acute episodes. Moderate elevations (e.g. < 3-fold) are more often due to medications or environmental factors. Source: Regenstrief LOINC

LP32067-8   Hemoglobin
Hemoglobin or haemoglobin [frequently abbreviated as Hb ] is the iron -containing oxygen -transport metalloprotein in the red cells of the blood in mammals and other animals. Hemoglobin in vertebrates transports oxygen from the lungs to the rest of the body, such as to the muscles, where it releases the oxygen load. Hemoglobin also has a variety of other gas-transport and effect-modulation duties, which vary from species to species, and which in invertebrates may be quite diverse. The name hemoglobin is the concatenation of heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme (or haem) group; each heme group contains an iron atom, and this is responsible for the binding of oxygen. The most common types of hemoglobin contains four such subunits, each with one heme group. 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 , Hemoglobin (Wikipedia)

LP32067-8   Hemoglobin
Hemoglobin (Hb or Hgb) is a protein in red blood cells that is responsible for transporting oxygen from the lungs to the body and transporting carbon dioxide back to the lungs. It is composed of two alpha subunits and two beta subunits non-covalently bonded.
Hemoglobin levels in the blood must be maintained to guarantee tissue oxygenation. A low concentration of hemoglobin is called anemia and can be caused either by a decreased number of erythrocytes (RBCs/red cells) in the blood or hyperhydration of the body. An increased concentration of hemoglobin can be caused either by a increased number of RBCs in the blood or dehydration of the body. [NCBI Books:NBK259] PMID: 20923558 Source: Regenstrief LOINC

LP32067-8   Hemoglobin
Hemoglobin is a protein inside red blood cells that transports oxygen throughout the body. It is made up of two alpha chains and two beta chains with a ring-shaped heme group that contains an atom of iron. The oxygen is picked up in the alveoli by the hemoglobin protein and binds reversibly to the iron atom. At the same time, carbon dioxide that was picked up in the tissues of the body is released into the lungs and exhaled. Hemoglobin variation is seen when the structure of the protein is altered due to a mutation such as in Hemoglobin S which causes sickle cell anemia. Hemoglobin variation can also result when there is a mismatch in the number of alpha and beta chains which leads to thalassemia.[http://pdb101.rcsb.org/motm/41] Source: Regenstrief LOINC

Fully-Specified Name

Component

Coproporphyrin/Hemoglobin

Property

MRto

Time

Pt

System

RBC

Scale

Qn

Method

Additional Names

Long Common Name

Coproporphyrin/Hemoglobin [Mass Ratio] in Red Blood Cells

Short Name

Copro/Hgb RBC

Display Name

Coproporphyrin/Hemoglobin (RBC) [Mass ratio]

Consumer Name Alpha Get Info

Coproporphyrin/Hemoglobin, Red blood cells

Basic Attributes

Class

CHEM

Type

Laboratory

First Released

Version 2.10

Last Updated

Version 2.70 (MIN)

Order vs. Observation

Observation

Language Variants Get Info

Related Names

• Chemistry
• Copro
• Coproporph
• Coproporphyrins
• Erythrocytes
• Haemoglobin
• Hb
• Hgb
• Mass concentration ratio
• Mass ratio
• MCRto
• Point in time
• QNT
• Quan
• Quant
• Quantitative
• Random
• Red blood cells
• Red blood corpusles
• Tetracarboxyl porphyrin
• Tetracarboxylporphyrin
• Tetracarboxylporphyrins
• Tetracarboxyporphyrin

Example Units

LOINC Terminology Service (API) using HL7^® FHIR^® Get Info

Requests to this service require a free LOINC username and password. Below is a sample of the possible capabilities. See the LOINC Terminology Service documentation for more information.

CodeSystem lookup

https://fhir.loinc.org/CodeSystem/$lookup?system=http://loinc.org&code=34402-8

LOINC Copyright

Copyright © 2025 Regenstrief Institute, Inc. All Rights Reserved. To the extent included herein, the LOINC table and LOINC codes are copyright © 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.