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Purification to homogeneity of camel pituitary pro-opiocortin, the common precursor of opioid peptides and corticotropin.
Author(s) -
Sadao Kimura,
Randolph V. Lewis,
Louise Gerber,
Larry Brink,
Menachem Rubinstein,
Stanley Stein,
Sidney Udenfriend
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.4.1756
Subject(s) - opioid peptide , peptide , chemistry , chromatography , opioid , pituitary gland , biochemistry , amino acid analysis , amino acid , receptor , hormone
Pro-opiocortin was purified from camel pituitaries by procedures including high-performance liquid chromatography. The precursor relationship of the pure protein to the opioid peptides and to corticotropin was confirmed. Partial chemical analysis consisting of amino acid analysis and tryptic peptide mapping was carried out with the aid of sensitive fluorescence detection.

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