Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 73 ·No. 4 ·1976-04-00 ·Pages 1145-8

Li CH, Chung D

Abstract

The isolation of an untriakontapeptide from camel pituitary extracts has been described. Its structure has been determined and shown to be identical to the sequence of carboxyl-terminal 31 amino acids of ovine beta-lipotropin. The peptide possesses very low lipotropic activity but significant opiate activity.

MeSH Terms

Amino Acids/analysis Animals Binding, Competitive Camelus Lipid Metabolism Morphine Oligopeptides/analysis Opium Peptides/analysis,isolation & purification,metabolism Pituitary Gland Receptors, Drug beta-Lipotropin/metabolism

Chemicals

Amino Acids Oligopeptides Peptides Receptors, Drug Morphine Opium beta-Lipotropin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Li C H

Chung D

References (15)

15 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.73.4.1145

Published

1976-04-00

Pages

1145-8

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC430217

Subset

External Links

PubMed source DOI: 10.1073/pnas.73.4.1145 PMC Full Text View journal details

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Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.

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