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rdf:type |
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lifeskim:mentions |
umls-concept:C0001655,
umls-concept:C0007625,
umls-concept:C0020792,
umls-concept:C0023832,
umls-concept:C0030956,
umls-concept:C0205214,
umls-concept:C0205345,
umls-concept:C0449830,
umls-concept:C1709634,
umls-concept:C1880022,
umls-concept:C1883254
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pubmed:issue |
12
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pubmed:dateCreated |
1978-3-21
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pubmed:abstractText |
Radioactive proteins synthesized in an mRNA-dependent reticulocyte cell-free system under the direction of mRNA from AtT-20/D-16v mouse cells were isolated by specific immunoprecipitation using antiserum to either alpha(1-24) corticotropin or beta-endorphin [beta(61-91) lipotropin]. Each immunoprecipitate was fractionated by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and shown to contain only one labeled protein with an apparent molecular weight of 28,500. Tryptic peptide analysis of the Mr 28,500 corticotropin and beta-lipotropin molecules isolated from the gels demonstrated that the two proteins had the same lysine, methionine, and tryptophan peptides. Four tryptic peptides from the cell-free product exhibited the same electrophoretic and chromatographic mobilities as marker tryptic peptides from bovine beta-melanotropin and porcine beta-endorphin. The identification of these peptides was confirmed by amino acid composition studies with a variety of labeled amino acids. The beta-lipotropin tryptic peptides were also shown to be located carboxy terminal to the corticotropin tryptic peptides.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-1063395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-1130680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-13723017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-180015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-180016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-197529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-200934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-266704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-267923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-4137932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-4294052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-4307702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-46869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-4949424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-823012,
http://linkedlifedata.com/resource/pubmed/commentcorrection/202948-883982
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5300-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:202948-Adrenocorticotropic Hormone,
pubmed-meshheading:202948-Amino Acid Sequence,
pubmed-meshheading:202948-Cell Line,
pubmed-meshheading:202948-Cell-Free System,
pubmed-meshheading:202948-Glycoproteins,
pubmed-meshheading:202948-Molecular Weight,
pubmed-meshheading:202948-Pituitary Gland,
pubmed-meshheading:202948-Polyribosomes,
pubmed-meshheading:202948-Protein Precursors,
pubmed-meshheading:202948-Reticulocytes,
pubmed-meshheading:202948-beta-Lipotropin
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pubmed:year |
1977
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pubmed:articleTitle |
Characterization of a common precursor to corticotropin and beta-lipotropin: identification of beta-lipotropin peptides and their arrangement relative to corticotropin in the precursor synthesized in a cell-free system.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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