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Isolation and structure of T-kinin
Biochemical and Biophysical Research Communications
|April 29, 1983
Summary
Researchers isolated T-kinin, a novel peptide related to bradykinin, from rat plasma. This peptide, isoleucyl-seryl-bradykinin, contracts the rat uterus and its structure was fully determined.
Area of Science:
- Biochemistry
- Peptide Chemistry
- Pharmacology
Background:
- Bradykinin is a peptide hormone with diverse physiological effects.
- Kininogens are precursors to kinins, including bradykinin.
- The existence of novel kinin variants is of interest in physiological research.
Purpose of the Study:
- To isolate and characterize a previously undescribed peptide from rat plasma.
- To determine the structure and biological activity of the isolated peptide.
- To investigate the relationship of its precursor to known kininogens.
Main Methods:
- Rat plasma was treated with trypsin.
- Peptide isolation utilized OM-cellulose, Biogel P-4, and reverse-phase high-performance liquid chromatography.
- Amino acid analysis and sequence determination were performed.
Main Results:
- A novel peptide, T-kinin, was isolated.
- T-kinin exhibits contractile activity on the rat uterus.
- The undecapeptide structure was determined as Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (isoleucyl-seryl-bradykinin).
Conclusions:
- T-kinin is a newly identified bradykinin-containing peptide.
- Its structure and uterotonic activity are characterized.
- Further investigation into T-kininogen's relationship with other kininogens is warranted.