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Descriptor English: Hemoglobin M
Descriptor Spanish: Hemoglobina M
Descriptor hemoglobina M
Scope note: Grupo de hemoglobinas anormales en las que tienen lugar muchas sustituciones de aminoácidos en las cadenas alfa o beta pero cerca del hierro heme. Este hecho da lugar a una mejor oxidación de la hemoglobina, que produce un exceso de methemoglobina, lo que lleva a cianosis.
Descriptor Portuguese: Hemoglobina M
Descriptor French: Hémoglobine M
Tree number(s): D12.776.124.400.463.510
D12.776.422.316.762.426.510
RDF Unique Identifier: https://id.nlm.nih.gov/mesh/D006449
Scope note: A group of abnormal hemoglobins in which amino acid substitutions take place in either the alpha or beta chains but near the heme iron. This results in facilitated oxidation of the hemoglobin to yield excess methemoglobin which leads to cyanosis.
Annotation: /urine: coordinate with HEMOGLOBINURIA
Allowable Qualifiers: AA analogs & derivatives
AD administration & dosage
AE adverse effects
AG agonists
AI antagonists & inhibitors
AN analysis
BI biosynthesis
CF cerebrospinal fluid
CH chemistry
CL classification
CS chemical synthesis
DE drug effects
DF deficiency
EC economics
GE genetics
HI history
IM immunology
IP isolation & purification
ME metabolism
PD pharmacology
PH physiology
PK pharmacokinetics
PO poisoning
RE radiation effects
SD supply & distribution
ST standards
TO toxicity
TU therapeutic use
UL ultrastructure
UR urine
Registry Number: 9083-28-7
CAS Type 1 Name: Hemoglobin M
Previous Indexing: Hemoglobins, Abnormal (1966-1976)
Public MeSH Note: 91; was see under HEMOGLOBINS, ABNORMAL 1977-90
History Note: 91(77); was see under HEMOGLOBINS, ABNORMAL 1977-90
Entry Version: HBM
DeCS ID: 22196
Unique ID: D006449
Documents indexed in the Virtual Health Library (VHL): Click here to access the VHL documents
Date Established: 1991/01/01
Date of Entry: 1976/04/27
Revision Date: 2016/06/28
Hemoglobin M - Preferred
Concept UI M0010123
Scope note A group of abnormal hemoglobins in which amino acid substitutions take place in either the alpha or beta chains but near the heme iron. This results in facilitated oxidation of the hemoglobin to yield excess methemoglobin which leads to cyanosis.
Preferred term Hemoglobin M



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