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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1984-5-11
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pubmed:abstractText |
Biosynthetically labeled reptile intermediate pituitary beta-endorphin-sized material was fractionated by SP-Sephadex ion exchange chromatography into two major opiate-active forms which eluted at 0.28 M NaCl and 0.32 M NaCl, respectively; the 0.32 M form of reptile beta-endorphin (mw = 3500), serves as the precursor for the 0.28 M form of reptile beta-endorphin (mw = 3200), (Dores and Surprenant, 1983). Analysis of tryptic digests of these reptile beta-endorphins by paper electrophoresis at pH 3.5 and gel filtration on a Sephadex G-15 column indicated that there are two tyrosine residues, two arginine residues and one methionine residue in reptile beta-endorphin. Furthermore, the NH2-terminal tryptic peptide of both reptile beta-endorphins is approximately nine amino acids in size and contains tyrosine, methionine and arginine. Analyses of chymotryptic/protease digests of the [3H]tyrosine-labeled NH2-terminal tryptic peptide analyzed by descending paper chromatography revealed that the NH2-terminal tyrosine of reptile beta-endorphin is not alpha-N-acetylated. A second tyrosine-containing tryptic peptide was detected in the COOH-terminal region of reptile beta-endorphin; however this tryptic peptide differs in the two forms of reptile beta-endorphin in terms of size and net charge at pH 3.5. These differences account for the apparent molecular weight differences and distinct ion exchange properties of the 0.28 M and 0.32 M forms of reptile beta-endorphin. Thus in the reptile intermediate pituitary the principal post-translational mechanism for modifying beta-endorphin is COOH-terminal proteolytic cleavage.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Endorphins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Endorphin
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pubmed:status |
MEDLINE
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pubmed:issn |
0196-9781
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
897-905
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6324142-Animals,
pubmed-meshheading:6324142-Chromatography, Gel,
pubmed-meshheading:6324142-Chymotrypsin,
pubmed-meshheading:6324142-Electrophoresis, Paper,
pubmed-meshheading:6324142-Endorphins,
pubmed-meshheading:6324142-Iguanas,
pubmed-meshheading:6324142-Lizards,
pubmed-meshheading:6324142-Male,
pubmed-meshheading:6324142-Peptide Fragments,
pubmed-meshheading:6324142-Pituitary Gland,
pubmed-meshheading:6324142-Trypsin,
pubmed-meshheading:6324142-beta-Endorphin
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pubmed:articleTitle |
Further characterization of the major forms of reptile beta-endorphin.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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