Related Experiment Video

Updated: Aug 8, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Ceruloplasmin receptors of erythrocytes

G Barnes, E Frieden

    Biochemical and Biophysical Research Communications
    |November 30, 1984
    PubMed

    More Related Videos

    Iridium(III) Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II12:52

    Iridium(III) Luminescent Probe for Detection of the Malarial Protein Biomarker Histidine Rich Protein-II

    Published on: July 7, 2015

    Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry07:20

    Measuring Erythrocyte Complement Receptor 1 Using Flow Cytometry

    Published on: May 19, 2020

    Related Concept Videos

    Directing Proteins to the Rough Endoplasmic Reticulum01:34

    Directing Proteins to the Rough Endoplasmic Reticulum

    The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
    Protein Modifications in the RER01:26

    Protein Modifications in the RER

    Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
    Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
    Erythropoiesis01:14

    Erythropoiesis

    Red blood cells  (RBCs) transport oxygen to all body tissues. These cells survive only for 120 days and then need to be replenished. Erythropoiesis is the process of RBC production. In healthy individuals, erythropoiesis ensures all tissues are amply supplied with oxygen. In addition, blood loss due to injury leads to a drop in the physiological oxygen level that will cause erythropoiesis. Any defect in erythropoiesis leads to several physiological disorders, including thalassemia, anemia, and...
    Structure and Function of Erythrocytes01:29

    Structure and Function of Erythrocytes

    There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
    The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
    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.
    Drug Binding to Blood Components01:30

    Drug Binding to Blood Components

    When drugs enter systemic circulation, they interact with various components of the blood, including proteins such as human serum albumin (HSA), α1-acid glycoprotein (AAG), lipoproteins, globulins, and red blood cells (RBCs).
    HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are further...