Isolation and amino acid sequence analysis of a 4,000-dalton dynorphin from porcine pituitary

A 4,000-dalton dynorphin was isolated from porcine pituitary. It has 32 amino acids (Mr= 3,986), with the previously described heptadecapeptide (now called dynorphin A) at its amino terminus and a related tridecapeptide, dynorphin B, at its carboxyl terminus. The two peptides are separated by the ``...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 79; no. 17; pp. 5435 - 5437
Main Authors Fischli, Walter, Goldstein, Avram, Hunkapiller, Michael W., Hood, Leroy E.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.09.1982
National Acad Sciences
Subjects
Adsorption
Amino Acid Sequence
Amino acids
Animals
Chromatography
Chromatography, High Pressure Liquid
dynorphin
Dynorphins
Endorphins - isolation & purification
Gels
Ileum
Molecular Weight
Opioid receptors
pigs
pituitary
Pituitary Gland - analysis
Radioimmunoassay
Receptors
Resins
Sodium
Swine
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Summary:A 4,000-dalton dynorphin was isolated from porcine pituitary. It has 32 amino acids (Mr= 3,986), with the previously described heptadecapeptide (now called dynorphin A) at its amino terminus and a related tridecapeptide, dynorphin B, at its carboxyl terminus. The two peptides are separated by the ``processing signal'' Lys-Arg.
Bibliography:L
L50
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.79.17.5435