Related Experiment Video

Updated: Jul 25, 2026

In Situ Ca2+ Imaging of the Enteric Nervous System
11:26

In Situ Ca2+ Imaging of the Enteric Nervous System

Published on: January 29, 2015

Subcellular localisation of di- and tripeptidases in guinea pig and rat enterocytes

G P Wells, J A Nicholson, T J Peters

    Biochimica Et Biophysica Acta
    |July 11, 1979
    PubMed

    More Related Videos

    Mixed Primary Cultures of Murine Small Intestine Intended for the Study of Gut Hormone Secretion and Live Cell Imaging of Enteroendocrine Cells09:16

    Mixed Primary Cultures of Murine Small Intestine Intended for the Study of Gut Hormone Secretion and Live Cell Imaging of Enteroendocrine Cells

    Published on: April 20, 2017

    Use of Anti-phospho-girdin Antibodies to Visualize Intestinal Tuft Cells in Free-Floating Mouse Jejunum Cryosections06:26

    Use of Anti-phospho-girdin Antibodies to Visualize Intestinal Tuft Cells in Free-Floating Mouse Jejunum Cryosections

    Published on: March 21, 2018

    Related Concept Videos

    The Early Endosome: Endocytosis of Transferrin01:28

    The Early Endosome: Endocytosis of Transferrin

    Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
    Post-translational Translocation of Proteins to the RER01:27

    Post-translational Translocation of Proteins to the RER

    A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
    Targeting proteins to the ER
    Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
    Protein Absorption01:12

    Protein Absorption

    Proteins in the gastrointestinal tract typically come from food, but they can also originate from disintegrated cells or secreted enzymes. In the stomach, the enzyme pepsin breaks down these proteins into polypeptides. The fragments then move into the duodenum as a semi-fluid mass called chyme. Pancreatic proteases, such as trypsin and chymotrypsin, and intestinal brush border enzymes like carboxypeptidases further dismantle the polypeptides into tripeptides, dipeptides, and free amino acids.