Specific binding of a 125I-labeled substance P analog to rat submaxillary gland

Suleiman Bahouth, J. M. Stewart, J. M. Musacchio

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The substance P (SP) analog [tyrosine1, norleucine11]-substance P ([Tyr1, Nle11]-SP) was iodinated by the chloramine-T method to yield the mono iodinated derivative; both peptides were biologically active on the guinea-pig ileum SP receptor. Saturable, reversible binding of [125I-Tyr1, Nle11]-SP to a single class of noninteracting sites on the rat submaxillary gland homogenate was demonstrated with an affinity of 9.26 ± 0.8 nM and a maximum binding 15.7 ± 1.25 or 250 ± 20 fmol/mg of protein. The relative potencies of SP and its fragments SP(2-11) and SP(4-11), as measured by their IC50, are in agreement with their rank order in the salivation assay, whereas physalaemin was found apparently weaker than expected. However, their rank order in displacing [125I-Tyr1, Nle11]-SP was identical to their rank order in displacing [125I-Bolton-Hunter]-SP bound to mouse mesencephalic cells in primary culture.

Original languageEnglish (US)
Pages (from-to)116-123
Number of pages8
JournalJournal of Pharmacology and Experimental Therapeutics
Volume230
Issue number1
StatePublished - Jan 1 1984
Externally publishedYes

Fingerprint

Submandibular Gland
Substance P
Physalaemin
Salivation
Neurokinin-1 Receptors
Primary Cell Culture
Ileum
Inhibitory Concentration 50
Guinea Pigs
Peptides

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Pharmacology

Cite this

Specific binding of a 125I-labeled substance P analog to rat submaxillary gland. / Bahouth, Suleiman; Stewart, J. M.; Musacchio, J. M.

In: Journal of Pharmacology and Experimental Therapeutics, Vol. 230, No. 1, 01.01.1984, p. 116-123.

Research output: Contribution to journalArticle

@article{c5cd7474186641fc865be8471d75664a,
title = "Specific binding of a 125I-labeled substance P analog to rat submaxillary gland",
abstract = "The substance P (SP) analog [tyrosine1, norleucine11]-substance P ([Tyr1, Nle11]-SP) was iodinated by the chloramine-T method to yield the mono iodinated derivative; both peptides were biologically active on the guinea-pig ileum SP receptor. Saturable, reversible binding of [125I-Tyr1, Nle11]-SP to a single class of noninteracting sites on the rat submaxillary gland homogenate was demonstrated with an affinity of 9.26 ± 0.8 nM and a maximum binding 15.7 ± 1.25 or 250 ± 20 fmol/mg of protein. The relative potencies of SP and its fragments SP(2-11) and SP(4-11), as measured by their IC50, are in agreement with their rank order in the salivation assay, whereas physalaemin was found apparently weaker than expected. However, their rank order in displacing [125I-Tyr1, Nle11]-SP was identical to their rank order in displacing [125I-Bolton-Hunter]-SP bound to mouse mesencephalic cells in primary culture.",
author = "Suleiman Bahouth and Stewart, {J. M.} and Musacchio, {J. M.}",
year = "1984",
month = "1",
day = "1",
language = "English (US)",
volume = "230",
pages = "116--123",
journal = "Journal of Pharmacology and Experimental Therapeutics",
issn = "0022-3565",
publisher = "American Society for Pharmacology and Experimental Therapeutics",
number = "1",

}

TY - JOUR

T1 - Specific binding of a 125I-labeled substance P analog to rat submaxillary gland

AU - Bahouth, Suleiman

AU - Stewart, J. M.

AU - Musacchio, J. M.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - The substance P (SP) analog [tyrosine1, norleucine11]-substance P ([Tyr1, Nle11]-SP) was iodinated by the chloramine-T method to yield the mono iodinated derivative; both peptides were biologically active on the guinea-pig ileum SP receptor. Saturable, reversible binding of [125I-Tyr1, Nle11]-SP to a single class of noninteracting sites on the rat submaxillary gland homogenate was demonstrated with an affinity of 9.26 ± 0.8 nM and a maximum binding 15.7 ± 1.25 or 250 ± 20 fmol/mg of protein. The relative potencies of SP and its fragments SP(2-11) and SP(4-11), as measured by their IC50, are in agreement with their rank order in the salivation assay, whereas physalaemin was found apparently weaker than expected. However, their rank order in displacing [125I-Tyr1, Nle11]-SP was identical to their rank order in displacing [125I-Bolton-Hunter]-SP bound to mouse mesencephalic cells in primary culture.

AB - The substance P (SP) analog [tyrosine1, norleucine11]-substance P ([Tyr1, Nle11]-SP) was iodinated by the chloramine-T method to yield the mono iodinated derivative; both peptides were biologically active on the guinea-pig ileum SP receptor. Saturable, reversible binding of [125I-Tyr1, Nle11]-SP to a single class of noninteracting sites on the rat submaxillary gland homogenate was demonstrated with an affinity of 9.26 ± 0.8 nM and a maximum binding 15.7 ± 1.25 or 250 ± 20 fmol/mg of protein. The relative potencies of SP and its fragments SP(2-11) and SP(4-11), as measured by their IC50, are in agreement with their rank order in the salivation assay, whereas physalaemin was found apparently weaker than expected. However, their rank order in displacing [125I-Tyr1, Nle11]-SP was identical to their rank order in displacing [125I-Bolton-Hunter]-SP bound to mouse mesencephalic cells in primary culture.

UR - http://www.scopus.com/inward/record.url?scp=0021287301&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021287301&partnerID=8YFLogxK

M3 - Article

VL - 230

SP - 116

EP - 123

JO - Journal of Pharmacology and Experimental Therapeutics

JF - Journal of Pharmacology and Experimental Therapeutics

SN - 0022-3565

IS - 1

ER -