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

ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
Bicarbonate-Carbonic Acid Buffer01:22

Bicarbonate-Carbonic Acid Buffer

The carbonic acid-bicarbonate buffer system is critical for maintaining the body's pH balance. It operates on the equilibrium:
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Renal Regulation of Acid-Base Balance01:29

Renal Regulation of Acid-Base Balance

Metabolic reactions in the body produce nonvolatile acids, such as sulfuric acid, which generate an acid load of approximately 1 mEq of H+ per kilogram of body weight daily. Excreting H+ in the urine is essential to balance this acid load.
In the kidneys, cells within the proximal convoluted tubules (PCT) and the collecting ducts secrete hydrogen ions (H+) into the tubular fluid. Specifically, in the PCT, Na+/H+ antiporters secrete H+ while reabsorbing Na+.
However, the intercalated cells in...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Roles of Electrolytes: Chloride and Bicarbonate01:29

Roles of Electrolytes: Chloride and Bicarbonate

Chloride ions contribute to the osmotic pressure gradient distinguishing the intracellular fluid (ICF) from the extracellular fluid (ECF). They counterbalance positively charged ions in the ECF and ensure its electrochemical stability. The renal system's process of chloride absorption and release generally mirrors that of sodium ions.
Conditions such as hypochloremia can arise from insufficient chloride reabsorption by the kidneys, often compounded by extended bouts of diarrhea, vomiting, or...

You might also read

Related Articles

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

Sort by
Same author

Trade-offs between ionic regulation and hypoxia tolerance in zebrafish (Danio rerio) raised in a low pH environment.

Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology·2026
Same author

Freshwater protected areas can preserve high-performance phenotypes in populations of a popular sportfish.

Conservation physiology·2023
Same author

Too stressed to eat: Investigating factors associated with appetite loss in subordinate rainbow trout.

Molecular and cellular endocrinology·2022
Same author

Role of cytosolic carbonic anhydrase Ca17a in cardiorespiratory responses to CO<sub>2</sub> in developing zebrafish (<i>Danio rerio)</i>.

American journal of physiology. Regulatory, integrative and comparative physiology·2022
Same author

Early-life stress influences ion balance in developing zebrafish (Danio rerio).

Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology·2020
Same author

The role of TASK-2 channels in CO<sub>2</sub> sensing in zebrafish (<i>Danio rerio</i>).

American journal of physiology. Regulatory, integrative and comparative physiology·2020

Related Experiment Video

Updated: Jun 12, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

Perspectives on carbonic anhydrase.

K M Gilmour1

  • 1Department of Biology, University of Ottawa, Ottawa, ON, Canada. kgilmour@uottawa.ca

Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology
|June 15, 2010
PubMed
Summary
This summary is machine-generated.

Carbonic anhydrase (CA) research has advanced significantly, yet understanding interspecific differences in red blood cell CA expression and activity remains crucial for physiological insights.

More Related Videos

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Related Experiment Videos

Last Updated: Jun 12, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

Published on: February 19, 2013

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
12:07

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

Published on: October 9, 2021

Area of Science:

  • Biochemistry
  • Physiology
  • Mammalian Biology

Background:

  • Red blood cell carbonic anhydrase (RBC CA) activity was previously studied in relation to body mass.
  • Knowledge of carbonic anhydrase (CA) has greatly expanded, revealing diverse isoforms and roles in physiological processes.

Purpose of the Study:

  • To highlight the ongoing relevance of questions regarding interspecific differences in CA expression and activity.
  • To underscore the need for further research into the physiological significance of these variations.

Main Methods:

  • Review of accumulated research over the past 50 years.
  • Analysis of established knowledge on CA catalytic mechanisms and identified activators/inhibitors.

Main Results:

  • CA is implicated in numerous physiological processes.
  • CA and its inhibitors show potential in diagnosing and treating diseases like glaucoma, cancer, and obesity.

Conclusions:

  • Despite extensive research, significant gaps remain in understanding mammalian CA diversity.
  • Further investigation into interspecific differences in CA expression and activity is essential.