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 Experiment Videos

Human red cell glyoxalase I polymorphism.

C W Parr, I A Bagster, S G Welch

    Biochemical Genetics
    |February 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Human erythrocyte glyoxalase I enzyme shows genetic variation through isoenzymatic forms. This polymorphism makes it a promising new genetic marker for research.

    Related Concept Videos

    You might also read

    Related Articles

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

    Sort by
    Same author

    Distribution of human kappa locus IGKV2-29 and IGKV2D-29 alleles in Swedish Caucasians and Hong Kong Chinese.

    Immunogenetics·2001
    Same author

    Progesterone 6-hydroxylation is catalysed by cytochrome P-450 in the moderate thermophile Bacillus thermoglucosidasius strain 12060.

    The Journal of steroid biochemistry and molecular biology·1999
    Same author

    Cloning and thermostability of TaqI endonuclease isoschizomers from Thermus species SM32 and Thermus filiformis Tok6A1.

    The Biochemical journal·1998
    Same author

    BstB7SI (R decreases CCGGY), a thermostable isoschizomer of Cfr10I, from a strain of Bacillus stearothermophilus isolated from oil-contaminated soil in Kuwait.

    FEMS microbiology letters·1998
    Same author

    Thermostable cytochrome P450 steroid hydroxylase from a thermophilic bacillus strain.

    Biochemical Society transactions·1997
    Same author

    Tsp49I (ACGT/), a thermostable neoschizomer of the Type II restriction endonuclease MaeII (A/CGT), discovered in isolates of the genus Thermus from the Azores, Iceland and New Zealand.

    Nucleic acids research·1996
    Same journal

    VALD-3 Induces GSDME-Dependent Pyroptosis via ROS/JNK/Bax Pathway in Triple-Negative Breast Cancer Cells.

    Biochemical genetics·2026
    Same journal

    Correlation Between SGK1 Expression Level and Multiple Myeloma Progression After Autologous Hematopoietic Stem Cell Transplantation.

    Biochemical genetics·2026
    Same journal

    Decoding Genetic Risk Factors in Recurrent Pregnancy Loss: An Integrative Chromosomal and Bioinformatics Approach.

    Biochemical genetics·2026
    Same journal

    Chromosome-Level Genome Assembly of the Sea Urchin Glyptocidaris crenularis and Sex Chromosome Identification.

    Biochemical genetics·2026
    Same journal

    Genetic Diversity and Population Structure of 72 Turkish Ficus carica (L.) Genotypes Assessed Using SCoT Markers.

    Biochemical genetics·2026
    Same journal

    A Splice-Site Variant in ACY1 Associated with Congenital Hearing Loss: Clinical, Biochemical, and Zebrafish Functional Evidence.

    Biochemical genetics·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Human Genetics
    • Enzymology

    Background:

    • Glyoxalase I is a crucial enzyme in the detoxification pathway of reactive carbonyl species.
    • Erythrocytes are readily accessible for biochemical analysis.
    • Understanding enzyme polymorphism is vital for population genetics and disease association studies.

    Purpose of the Study:

    • To investigate the isoenzymatic forms of human erythrocyte glyoxalase I.
    • To develop a reliable method for visualizing these isoenzymes.
    • To assess the potential of glyoxalase I as a genetic marker.

    Main Methods:

    • Starch gel electrophoresis was employed to separate glyoxalase I isoenzymes.
    • A novel positive staining technique was utilized for isoenzyme visualization.

    Related Experiment Videos

  • Human erythrocyte lysates were analyzed.

    • Main Results:

    • The study successfully identified distinct isoenzymatic forms of human erythrocyte glyoxalase I.
    • The developed staining procedure provided clear visualization of these enzyme variants.
    • Evidence of glyoxalase I polymorphism in the human erythrocyte system was established.

    Conclusions:

    • Human erythrocyte glyoxalase I exhibits significant polymorphism.
    • The identified isoenzymes can serve as valuable genetic markers.
    • This finding opens avenues for population genetic studies and marker-assisted research.