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Dipeptide transport in isolated intestinal brush border membrane
Biochimica Et Biophysica Acta
|June 25, 1975
Summary
Glycyl-L-leucine is transported intact via a specific dipeptide mechanism, not as individual amino acids. This mechanism is distinct from amino acid transporters and is influenced by sodium ions.
Area of Science:
- Biochemistry
- Molecular Biology
- Physiology
Background:
- Dipeptide transport across the brush border membrane is crucial for nutrient absorption.
- Understanding the specific mechanisms involved is key to comprehending intestinal physiology.
Purpose of the Study:
- To investigate the transport mechanism of glycyl-L-leucine in isolated brush border membrane vesicles.
- To determine if glycyl-L-leucine is transported intact or as its constituent amino acids.
Main Methods:
- Studied the transport kinetics of glycyl-L-leucine in isolated brush border membrane vesicles.
- Examined the effects of sodium ions, individual amino acids (glycine, L-leucine), and other dipeptides on glycyl-L-leucine uptake.
Main Results:
- Glycyl-L-leucine transport exhibited a different time course and sodium dependency compared to glycine and L-leucine.
- Glycine and L-leucine did not inhibit glycyl-L-leucine transport, but other dipeptides did.
- The dipeptide was found within the vesicle initially, and its presence accelerated amino acid uptake.
Conclusions:
- Glycyl-L-leucine is transported intact by a specific dipeptide transport system.
- This dipeptide mechanism is distinct from individual amino acid transporters.
- The dipeptide transporter may play a role in overall amino acid absorption.