Bovine pineal antireproductive tripeptide binds to luteinizing hormone-releasing hormone: a model for peptide modulation by sequence specific peptide interactions?

Abstract:

:We report results of chromatographic, pH titration and nuclear magnetic resonance (NMR) spectroscopy studies demonstrating that the bovine pineal antireproductive tripeptide, Thr-Ser-Lys (BPART), binds to luteinizing hormone-releasing hormone (LHRH) at a site comprised of LHRH 2-5 (His-Trp-Ser-Tyr). BPART and LHRH have been shown to be antagonists in vitro. The binding constant is ca. 2 X 10(3)/mole. An NMR study of fifty other peptide pairs demonstrates that the binding is sequence and residue specific. The binding provides evidence of the amino acid pairing hypothesis, and suggests the possibility of modulation of one peptide by directly binding with another peptide.

journal_name

Brain Res Bull

journal_title

Brain research bulletin

authors

Root-Bernstein RS,Westall FC

doi

10.1016/0361-9230(86)90219-4

subject

Has Abstract

pub_date

1986-10-01 00:00:00

pages

519-28

issue

4

eissn

0361-9230

issn

1873-2747

pii

0361-9230(86)90219-4

journal_volume

17

pub_type

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