Isolation of a heptapeptide Val‐Val‐Tyr‐Pro‐Trp‐Thr‐Gln (valorphin) with some opiate activity

Wiley - Tập 39 Số 6 - Trang 477-484 - 1992
Judit Érchegyi1,2, Abba J. Kastin2, James E. Zadina2, X. Qiu3,2
1On leave of absence from the 1st Institute of Biochemistry, Semmelweis University School of Medicine, Budapest, Hungary 1088.
2VA Medical Center and Tulane University School of Medicine, New Orleans, LA, USA
3On leave of absence from the Shanghai Institute of biochemistry, Academia Sinica, Shanghai, China 200031.

Tóm tắt

Bovine hypothalamic tissue was extracted and purified by solid phase extraction and several reversed‐phase HPLC steps. The amino acid sequence of the purified peptide was determined by Edman degradation to be Val‐Val‐Tyr‐Pro‐Trp‐Thr‐Gln. This was confirmed by comparison of its chromatographic behavior with that of the synthetic peptide, and mass spectrometric analysis resulted in a mass identical to the calculated mass for this peptide. This heptapeptide shows homology with residues 32‐38 of the beta‐chain of bovine hemoglobin. The peptide inhibited the electrically induced contractions of the guinea pig ileum muscle preparation; this inhibition was reversible by naloxone. It also inhibited the binding of 125I‐DAMGO (selective for μ receptors) to rat brain with an IC50 of 10 μm and the binding of 3H‐DPDPE (selective for σ receptors) with an IC50 of 185 μm. With two valines at the N‐terminus and some opiate activity, valorphin seems a suitable name for this newly isolated peptide.

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Wiley

Tập 39 Số 6

477-484

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