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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1989-6-8
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pubmed:abstractText |
The reaction of endoproteinase Arg-C on the skeletal myosin head heavy chain was investigated through characterization of peptides and amino acid sequence analysis. The protease splits exclusively the 50 kDa-20 kDa junction at the lysine cluster spanning residues 639-641 and does not affect any other protease-sensitive region of the entire myosin heavy chain. The sensitivity of the cleavage to actin and nucleotide binding makes this protease a very specific conformational probe of S-1. The nicked S-1 derivative, containing an intact NH2-terminal 75 kDa fragment, may serve as a tool for gaining further insights into the domain structure and function of the myosin head.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/1,5-I-AEDANS,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Ca(2 ) Mg(2 )-ATPase,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Subfragments,
http://linkedlifedata.com/resource/pubmed/chemical/Myosins,
http://linkedlifedata.com/resource/pubmed/chemical/Naphthalenesulfonates,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/submandibular proteinase A
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
246
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
171-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2523317-Actins,
pubmed-meshheading:2523317-Adenosine Triphosphate,
pubmed-meshheading:2523317-Animals,
pubmed-meshheading:2523317-Ca(2+) Mg(2+)-ATPase,
pubmed-meshheading:2523317-Cross-Linking Reagents,
pubmed-meshheading:2523317-Endopeptidases,
pubmed-meshheading:2523317-Fluorescent Dyes,
pubmed-meshheading:2523317-Lysine,
pubmed-meshheading:2523317-Molecular Weight,
pubmed-meshheading:2523317-Myosin Subfragments,
pubmed-meshheading:2523317-Myosins,
pubmed-meshheading:2523317-Naphthalenesulfonates,
pubmed-meshheading:2523317-Peptide Fragments,
pubmed-meshheading:2523317-Protein Conformation,
pubmed-meshheading:2523317-Rabbits,
pubmed-meshheading:2523317-Serine Endopeptidases,
pubmed-meshheading:2523317-Trypsin
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pubmed:year |
1989
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pubmed:articleTitle |
Selective cleavage at lysine of the 50 kDa-20 kDa connector loop segment of skeletal myosin S-1 by endoproteinase Arg-C.
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pubmed:affiliation |
Centre de Recherches de Biochimie Macromoléculaire du CNRS, INSERM U249, Université de Montpellier, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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