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

Renal carbonic anhydrase.

D C Dobyan, R E Bulger

    The American Journal of Physiology
    |October 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    This study details renal carbonic anhydrase (CA), a zinc enzyme vital for kidney function. Researchers identified two CA isozymes in mammalian kidneys, crucial for urinary acidification and bicarbonate reabsorption.

    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

    Gap junctions occur in vertebrate renal proximal tubule cells.

    The Journal of cell biology·2009
    Same author

    The healthcare ethics committee in the structural transformation of health care: administrative and organization ethics in changing times.

    HEC forum : an interdisciplinary journal on hospitals' ethical and legal issues·1998
    Same author

    Toward a statement of the principles underlying responsible conduct in biomedical research.

    Academic medicine : journal of the Association of American Medical Colleges·1994
    Same author

    Studying science in the context of ethics.

    Academic medicine : journal of the Association of American Medical Colleges·1993
    Same author

    Renal malacoplakia reappraised.

    American journal of kidney diseases : the official journal of the National Kidney Foundation·1993
    Same author

    Obstacles to collegiality in the academic health center.

    Bulletin of the New York Academy of Medicine·1992

    Area of Science:

    • Biochemistry
    • Physiology
    • Enzymology

    Background:

    • Carbonic anhydrase (CA) is a ubiquitous zinc metalloenzyme involved in crucial physiological processes.
    • Mammalian kidneys exhibit multiple CA isozymes, with significant research advancements in understanding renal CA over the past decade.
    • Renal CA is hypothesized to play a key role in urinary acidification and bicarbonate reabsorption.

    Purpose of the Study:

    • To characterize the nature and distribution of carbonic anhydrase isozymes in the mammalian kidney.
    • To elucidate the biochemical and morphological properties of renal carbonic anhydrases.
    • To explore the potential physiological roles of renal carbonic anhydrases in different nephron segments.

    Main Methods:

    • Biochemical analysis of carbonic anhydrase activity.

    Related Experiment Videos

  • Morphological studies including histochemistry and immunocytochemistry.
  • Fractionation of kidney homogenates to isolate enzyme forms.
  • Main Results:

    • Two distinct carbonic anhydrase isozymes identified in the mammalian kidney: a soluble cytoplasmic form and a membrane-bound form.
    • The soluble cytoplasmic form (similar to erythrocyte CA C) constitutes the majority of renal CA activity.
    • The membrane-bound form, representing 2-5% of renal activity, is localized in brush border and basolateral fractions.
    • Histochemical and immunocytochemical studies reveal heterogeneous distribution of these isozymes along the nephron and collecting duct.

    Conclusions:

    • Mammalian kidneys possess at least two distinct carbonic anhydrase isozymes with differential localization.
    • The soluble and membrane-bound renal CA isozymes likely contribute to specific functions in different segments of the nephron and collecting duct system.
    • Further investigation into the distinct physiological roles of these renal carbonic anhydrases is warranted.