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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
1988-7-12
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pubmed:abstractText |
A polypeptide homologous to human and mouse J chain has been identified in the high molecular weight (HMW) Ig of the bullfrog, Rana catesbeiana. In previous studies, we had detected a component that was similar in size to mammalian J chains and that, relative to L chains, migrated rapidly to the anode in alkaline-urea PAGE; however, its mobility was less than that of mammalian J chains. We now demonstrate that this component is covalently linked to the H chain of R. catesbeiana HMW Ig. All of the disulfide bridges of this polypeptide, like those of human and mouse J chain, can be cleaved by reducing agents even in the absence of denaturing solvents. The putative frog J chain was isolated by a procedure that did not require preliminary purification of the HMW Ig. The chain differed in amino acid composition from L chains but resembled J chains from several other species. Tryptic peptides were isolated and sequenced. Except for a single heptapeptide, the peptides could be aligned by virtue of their similarity to segments of human and mouse J chain. Of the 116 residues that were placed, 55 were identical with residues in human J chain and 60 with residues in mouse J chain. The six cysteine residues identified in the frog J chain are at the same positions as six of the eight cysteines in the human and mouse J chains. The results indicate significant conservation in structure between amphibian and mammalian Ig J chains.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin J-Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
140
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4279-85
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3131430-Amino Acid Sequence,
pubmed-meshheading:3131430-Amino Acids,
pubmed-meshheading:3131430-Animals,
pubmed-meshheading:3131430-Biopolymers,
pubmed-meshheading:3131430-Disulfides,
pubmed-meshheading:3131430-Humans,
pubmed-meshheading:3131430-Immunoglobulin Heavy Chains,
pubmed-meshheading:3131430-Immunoglobulin J-Chains,
pubmed-meshheading:3131430-Macromolecular Substances,
pubmed-meshheading:3131430-Mice,
pubmed-meshheading:3131430-Molecular Sequence Data,
pubmed-meshheading:3131430-Molecular Weight,
pubmed-meshheading:3131430-Protein Denaturation,
pubmed-meshheading:3131430-Rana catesbeiana
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pubmed:year |
1988
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pubmed:articleTitle |
J chain in Rana catesbeiana high molecular weight Ig.
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pubmed:affiliation |
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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