Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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...
Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
RNA Editing02:23

RNA Editing

RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...
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...
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.
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The effect of albumin, ceruloplasmin, and other serum constitutents on Fe(II) oxidation.

Biological trace element research·2013
Same author

Identification of citrate as the albumin-bound inhibitor of the ferroxidase activity of ceruloplasmin.

Biological trace element research·2013
Same author

The effect of copper ion on glutathione and hemolysis in rabbit erythrocytes.

Biological trace element research·2013
Same author

Partial purification of the rat erythrocyte ceruloplasmin receptor monitored by an electrophoresis mobility shift assay.

Analytical biochemistry·1993
Same author

A tentacle gel simplifies the purification of ceruloplasmin.

Biochemistry international·1992
Same author

Thyroid hormone receptor induction by triiodothyronine in tadpole erythrocytes in vivo and in vitro and the effect of cycloheximide and actinomycin-D.

General and comparative endocrinology·1992

Related Experiment Video

Updated: Jul 12, 2026

Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs
06:12

Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs

Published on: January 27, 2021

Hemoglobin: molecular changes during anuran metamorphosis.

C D TRADER, J S WORTHAM, E FRIEDEN

    Science (New York, N.Y.)
    |March 8, 1963
    PubMed
    Summary

    During anuran metamorphosis, frog red blood cells undergo significant hemoglobin changes. Tadpoles shift from lighter 4.3S hemoglobin to a heavier 7.0S component, altering their blood composition.

    Area of Science:

    • Biochemistry
    • Developmental Biology
    • Comparative Physiology

    Background:

    • Anuran metamorphosis involves profound physiological and biochemical transformations.
    • Red blood cell (RBC) composition changes during amphibian development.
    • Hemoglobin (Hb) is crucial for oxygen transport and can vary significantly between developmental stages.

    Purpose of the Study:

    • To investigate alterations in hemoglobin sedimentation patterns during anuran metamorphosis.
    • To characterize the molecular changes in hemoglobin during the transition from tadpole to adult frog.
    • To correlate changes in hemoglobin composition with observed electrophoretic mobility shifts.

    Main Methods:

    • Analysis of red blood cell lysates from Rana grylio and Rana catesbeiana tadpoles and adult frogs.
    Keywords:
    FROGSHEMOGLOBIN

    More Related Videos

    Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos
    06:57

    Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

    Published on: July 21, 2021

    Optimized Analysis of Proteins from Xenopus Oocytes and Embryos by Immunoblotting
    09:32

    Optimized Analysis of Proteins from Xenopus Oocytes and Embryos by Immunoblotting

    Published on: September 19, 2025

    Related Experiment Videos

    Last Updated: Jul 12, 2026

    Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs
    06:12

    Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs

    Published on: January 27, 2021

    Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos
    06:57

    Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

    Published on: July 21, 2021

    Optimized Analysis of Proteins from Xenopus Oocytes and Embryos by Immunoblotting
    09:32

    Optimized Analysis of Proteins from Xenopus Oocytes and Embryos by Immunoblotting

    Published on: September 19, 2025

  • Sedimentation velocity ultracentrifugation to determine hemoglobin component sizes.
  • Amino acid composition analysis of hemoglobins.
  • Electrophoresis to assess protein mobility.

    • Main Results:

    • Tadpole hemoglobins primarily consist of a 4.3S component (MW 68,000).
    • During metamorphosis, a heavier 7.0S component (estimated MW 136,000) is progressively produced.
    • Significant changes in amino acid composition were observed between tadpole and adult hemoglobins.
    • These compositional changes correlate with altered electrophoretic mobilities.

    Conclusions:

    • Anuran metamorphosis is characterized by a shift in hemoglobin composition, involving the production of a dimeric or tetrameric form of hemoglobin.
    • Changes in amino acid sequences drive alterations in hemoglobin structure and function during development.
    • These molecular adaptations are essential for meeting the changing oxygen demands of the developing frog.