Related Experiment Video

Updated: May 27, 2026

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
10:33

Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow

Published on: January 8, 2014

Isolation and functional characterization of hemoglobin Casper: beta106(G8) Leu replaced by Pro

H Wajcman, G Gacon, D Labie

    Biochemistry
    |November 4, 1975
    PubMed

    Insights

    Hemoglobin Casper, an abnormal variant, exhibits high oxygen affinity and altered Bohr effect. Its oxygen binding is independent of other hemoglobin molecules, suggesting no hybrid formation.

    Area of Science:

    • Biochemistry
    • Hematology
    • Molecular Biology

    Background:

    • Hemoglobinopathies represent a group of genetic disorders affecting hemoglobin structure and function.
    • Hemoglobin Casper is a rare variant characterized by a specific amino acid substitution.
    • Understanding the functional consequences of hemoglobin variants is crucial for diagnosing and managing related anemias.

    Purpose of the Study:

    • To characterize the physicochemical and functional properties of Hemoglobin Casper (beta106Leu replaced by Pro).
    • To determine the prevalence and oxygen-binding characteristics of Hemoglobin Casper in affected individuals.
    • To investigate the interaction between Hemoglobin Casper and normal Hemoglobin A.

    Main Methods:

    • Isoelectric focusing on polyacrylamide gel electrophoresis for separation and quantification.
    • Heat lability kinetics assay to assess stability.
    • Oxygen equilibrium curve analysis to determine oxygen affinity and Bohr effect.
    • Spectrophotometric methods to analyze subunit interactions.

    Main Results:

    • Hemoglobin Casper was successfully separated from Hemoglobin A using isoelectric focusing.
    • This abnormal hemoglobin constituted approximately 30% of the total hemoglobin.
    • Oxygen equilibrium studies revealed high oxygen affinity, reduced subunit interaction, and a diminished Bohr effect for Hemoglobin Casper.
    • Mixtures of Hemoglobin Casper and Hemoglobin A did not exhibit cooperative oxygen binding, indicating a lack of hybrid molecule formation.

    Conclusions:

    • Hemoglobin Casper possesses distinct functional properties, including high oxygen affinity and an impaired Bohr effect.
    • The absence of hybrid molecule formation in mixtures suggests unique quaternary structure dynamics.
    • These findings contribute to the understanding of hemoglobin variant pathophysiology and their clinical implications.

    More Related Videos

    Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP009208:53

    Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

    Published on: October 2, 2017

    Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry05:45

    Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry

    Published on: June 8, 2021

    Related Concept Videos

    Multiple Allele Traits01:49

    Multiple Allele Traits

    The Concept of Multiple Allelism
    Protein and Protein Structure02:15

    Protein and Protein Structure

    Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
    A protein's shape is critical to its function. For example, an enzyme can...
    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...
    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...