Related Experiment Video

Updated: Jul 10, 2026

Magnetic Levitation Coupled with Portable Imaging and Analysis for Disease Diagnostics
07:42

Magnetic Levitation Coupled with Portable Imaging and Analysis for Disease Diagnostics

Published on: February 19, 2017

Denatured hemoglobin in sickle erythrocytes

T Asakura, K Minakata, K Adachi

    The Journal of Clinical Investigation
    |April 1, 1977
    PubMed

    To study the nature of numerous inclusion bodies seen in red cells from patients with sickle cell disease (Hb SS), we have prepared red cell ghosts free of oxyhemoglobin and analyzed them by spectrophotometric and heme extraction methods. The absorption spectrum in the visible region of the ghost suspensions was typical of hemichromes. The spectrum was similar to that of denatured hemoglobin repared by treatment of oxyhemoglobin S with mechanical shaking or heat. Similar treatment of cells containing only normal hemoglobin (Hb AA) showed a very small amount of denatured hemoglobin, approximately one-fifth of the amount in Hb SS cells. The amount of denatured hemoglobin determined after solution of membrane with 2.5% sodium dodecyl sulfate was 0.158+/-0.070% (1 SD) of the total cellular heme in Hb SS patients. In controls, the amount was 0.030+/-0.016%. Persons with Hb AA and reticulocytosis did not have an elevated amount of membrane-associated heme. In patients with hereditary spherocytosis and autoimmune hemolytic anemia, denatured stromal hemoglobin was normal or slightly elevated before and after splenectomy. The increased amount of denatured hemoglobin in Hb SS red cells may be related to the instability of sickle oxyhemoglobin.

    More Related Videos

    Measuring Deformability and Red Cell Heterogeneity in Blood by Ektacytometry09:12

    Measuring Deformability and Red Cell Heterogeneity in Blood by Ektacytometry

    Published on: January 12, 2018

    Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry08:23

    Characterization of Sickling During Controlled Automated Deoxygenation with Oxygen Gradient Ektacytometry

    Published on: November 5, 2019

    Related Concept Videos

    Multiple Allele Traits01:49

    Multiple Allele Traits

    The Concept of Multiple Allelism
    Protein Denaturation01:28

    Protein Denaturation

    The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
    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...
    Lifecycle of Erythrocytes01:22

    Lifecycle of Erythrocytes

    Erythrocytes, also known as red blood cells, constantly move through blood capillaries. As a result, they damage their plasma membrane due to the continuous friction. Typically, after 100 to 120 days, erythrocytes become rigid and fragile as they wear out. As they pass through small vessels in the spleen and liver, they can get trapped and break apart into fragments.
    The resident phagocytic macrophages deal with these damaged cells by engulfing them and separating their globin and heme groups.
    Disorders of Erythrocytes01:27

    Disorders of Erythrocytes

    Disorders of erythrocytes, or red blood cells (RBCs), include a range of conditions affecting their number, shape, or function.
    Erythrocyte disorders can be broadly categorized into two main types: anemic and polycythemic conditions.
    A low oxygen-carrying capacity of the blood due to the loss, lower production, or destruction of erythrocytes is termed anemia. Hemorrhagic anemia, for example, occurs when bleeding from an external wound or internal ulcer reduces erythrocyte counts.
    On the other...
    Oxygen Transport in the Blood01:27

    Oxygen Transport in the Blood

    Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...