Structured Summary
Abstract
Metalloproteins that function as oxygen transport proteins in the HEMOLYMPH of MOLLUSKS and ARTHROPODS. They are characterized by two copper atoms, coordinated with HISTIDINE residues, that reversibly bind a single oxygen molecule; they do not contain HEME groups.
MeSH Record
Classification
Broader headings
Related Concepts
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MeSH Record
Synonyms
7 entry terms
- Hemocyanin
- alpha-Haemocyanin
- alpha-Hemocyanin
- alpha-Hemocyanins
- alpha Haemocyanin
- alpha Hemocyanin
- alpha Hemocyanins
MeSH Record
Aspects Covered
30 allowable subheadings
Indexed with the subheadings administration & dosage, adverse effects, agonists, analysis, antagonists & inhibitors, biosynthesis, blood, cerebrospinal fluid, chemical synthesis, chemistry, classification, deficiency, drug effects, economics, genetics, history, immunology, isolation & purification, metabolism, pharmacokinetics, pharmacology, physiology, poisoning, radiation effects, standards, supply & distribution, therapeutic use, toxicity, ultrastructure, urine.
MeSH Record
History Note
2018 (1964)
MeSH Hierarchy
Tree Numbers
MeSH Record
NLM Classification
QU 55.8
AMA Style
References
- National Library of Medicine. Hemocyanins. Medical Subject Headings (MeSH). 2026. Unique ID D006433. http://id.nlm.nih.gov/mesh/2026/D006433
- Hemocyanins. In: Wikipedia. https://en.wikipedia.org/wiki/Hemocyanin
- Hemocyanins. In: Wikidata. https://www.wikidata.org/wiki/Q407688