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Hemoglobin

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Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
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Related Experiment Video

Updated: Jun 26, 2026

A Precise and Quantifiable Method for Collecting Hemolymph from Small Arthropods

A Precise and Quantifiable Method for Collecting Hemolymph from Small Arthropods

Published on: April 28, 2023

Heme-binding storage proteins in the Chelicerata.

Kevin V Donohue¹, Sayed M S Khalil, Daniel E Sonenshine

¹Department of Entomology, Campus Box 7647, North Carolina State University, Raleigh, NC 27695-7647, USA.

Journal of Insect Physiology

|February 3, 2009

Summary

Chelicerata lipoglycoproteins, like carrier proteins (CP) and vitellogenins (Vg), uniquely bind and store heme, mitigating toxicity and aiding reproduction. This heme-binding capability is crucial for hematophagy evolution.

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Area of Science:

Biochemistry
Evolutionary Biology
Arthropod Physiology

Background:

Heme-binding storage proteins in Chelicerata, such as vitellogenins (Vg) and carrier proteins (CP), represent a unique evolutionary strategy.
Knowledge of these proteins is limited, with current understanding derived from studies on ixodid ticks and the black widow spider (Latrodectus mirabilis).

Purpose of the Study:

To explore the evolutionary significance and function of heme-binding storage proteins in Chelicerata.
To compare heme-binding proteins across different arachnid species and with non-chelicerate arthropods.

Main Methods:

Analysis of lipoglycoproteins, including vitellogenins (Vg) and carrier proteins (CP), in Chelicerata.
Comparison of primary structure and post-translational processing of tick CP and Vg.
Characterization of high-density lipoprotein 1 (HDL1) from Latrodectus mirabilis.

Main Results:

Tick CP and L. mirabilis HDL1 share similarities, including subunit composition, hemolymph dominance, and binding of lipids, carbohydrates, and cholesterol.
CP binds heme; HDL1 likely does as well, indicated by a brown pigment.
CP is structurally related to Vg but differs in post-translational processing.

Conclusions:

Heme-binding storage proteins in Chelicerata, particularly CP and Vg, play a vital role in managing heme toxicity and utilizing it as a prosthetic group.
These proteins are critical for reproduction, blood-feeding, and development, potentially driving the evolution of hematophagy.