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Related Concept Videos

Hemoglobin01:24

Hemoglobin

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.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...

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Related Experiment Video

Updated: Jul 7, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Mini-hemoglobins from nemertean worms.

Thomas L Vandergon1, Austen F Riggs

  • 1Natural Science Division, Pepperdine University, Malibu, California, USA.

Methods in Enzymology
|February 2, 2008
PubMed
Summary

Researchers detail methods for isolating and purifying unique, small hemoglobins (Hbs) from nemertean worms. These mini-Hbs, found in nerve, muscle, and blood cells, possess interesting structural and binding properties.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Zoology

Background:

  • Nemertean hemoglobins (Hbs) are exceptionally small compared to other known Hb molecules.
  • These mini-Hbs exhibit unique structural characteristics and stable ligand-binding capabilities.
  • Expression of mini-Hb is observed in diverse tissues, including neural, muscle, and red blood cells.

Purpose of the Study:

  • To outline methodologies for the isolation and purification of functional mini-Hbs.
  • To provide a protocol applicable to multiple tissue types in nemertean worms.

Main Methods:

  • Tissue-specific extraction protocols.
  • Protein purification techniques (e.g., chromatography).
  • Functional assays to confirm Hb activity.

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A Precise and Quantifiable Method for Collecting Hemolymph from Small Arthropods

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Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
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Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Published on: January 31, 2022

Related Experiment Videos

Last Updated: Jul 7, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

A Precise and Quantifiable Method for Collecting Hemolymph from Small Arthropods
03:39

A Precise and Quantifiable Method for Collecting Hemolymph from Small Arthropods

Published on: April 28, 2023

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay
05:08

Measurement of Tissue Non-Heme Iron Content using a Bathophenanthroline-Based Colorimetric Assay

Published on: January 31, 2022

Main Results:

  • Successful isolation of functional mini-Hbs from neural, muscle, and red blood cell tissues.
  • Characterization of purification efficiency and Hb stability.

Conclusions:

  • Established methods enable the recovery of functional nemertean mini-Hbs.
  • These techniques facilitate further research into the structure-function relationships of these unique proteins.