Related Experiment Video
Updated: Aug 12, 2026

13:04
Atomic Absorbance Spectroscopy to Measure Intracellular Zinc Pools in Mammalian Cells
Published on: May 16, 2019
Zinc transfer among proteins in rat duodenum mucosa
Annals of Nutrition & Metabolism
|January 1, 1987
Summary
Zinc absorption in rat duodenum involves rapid passive binding to a 6,500 MW protein, followed by an active transfer to a 45,000 MW protein. This process is influenced by metabolic activity.
Area of Science:
- Gastrointestinal Physiology
- Trace Element Metabolism
- Biochemistry
Background:
- Zinc is an essential trace element crucial for numerous cellular functions.
- Understanding the mechanisms of zinc absorption in the gastrointestinal tract is vital for nutritional science.
- The initial steps of zinc uptake and intracellular transport remain incompletely elucidated.
Purpose of the Study:
- To investigate the kinetics of zinc binding to mucosal proteins in the rat duodenum.
- To identify the molecular weight of proteins involved in intracellular zinc transport.
- To determine whether zinc uptake and transfer processes are passive or active.
Main Methods:
- Incubation of rat duodenal tissue with 65ZnCl2 for short durations (5-60 seconds).
- Separation and fractionation of mucosal cytosol using gel filtration chromatography (Sephadex G-75).
- Quantification of 65Zn distribution among protein fractions based on molecular weight.
Main Results:
- 65Zn was primarily associated with two protein fractions, approximately 45,000 and 6,500 molecular weight.
- The ratio of 65Zn bound to the 45,000 MW protein versus the 6,500 MW protein increased with incubation time.
- Metabolic inhibitors significantly reduced the 65Zn ratio favoring the larger protein, indicating an active process.
Conclusions:
- Zinc enters the duodenal mucosal cytoplasm and rapidly binds passively to a 6,500 MW protein.
- Subsequently, zinc is actively transferred from the smaller protein to a 45,000 MW protein.
- This suggests a two-step mechanism for intracellular zinc handling during absorption, involving both passive and active transport components.
Related Concept Videos
Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Transcytosis of IgG
Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...

