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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1995-7-5
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pubmed:abstractText |
Calretinin is an EF-hand Ca(2+)-binding protein expressed predominantly in some neurons. We have found that the tryptic digestion pattern of rat recombinant calretinin depends on Ca2+ concentration as determined by SDS/PAGE, amino-acid-sequence analysis and electrospray-ionization MS. Ca(2+)-saturated calretinin was cleaved between amino acids 60 and 61 to yield two fragments, which accumulated during cleavage. Small amounts of the larger fragment (amino acid residues 61-271) were further cleaved from the C-terminal end. Ca(2+)-free calretinin was also cleaved between residues 60 and 61; however, under the latter conditions the fragment 61-271 was further cleaved from the N-terminal end. Native rat calretinin was cleaved by trypsin in a similar Ca(2+)-dependent fashion. All identified fragments of recombinant calretinin bound 45Ca2+ on nitrocellulose filters, although to a different extent. The 61-271 fragment was released by EGTA from an octyl-agarose column in a manner similar to intact calretinin, while fragment 61-233 was not eluted by EGTA. These observations show that there are trypsin cleavage sites in calretinin that are available regardless of Ca2+ binding, other sites that are completely protected against trypsin on Ca(2+)-binding and sites which become partially available on Ca(2+)-binding. Together these data show that calretinin changes its conformation on Ca2+ binding and identify the regions which are exposed in apo and Ca(2+)-bound form.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1381122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1384200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1397083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1407555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1420337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1473275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1488126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1505001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1664495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1715238,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1939729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1947178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-1988053,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2001709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2016417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2058003,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2140897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2191560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2479149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2508225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2602362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-2673026,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-3454274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-3654755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-6715311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-7093699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-7918640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-8054853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-8344307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-8407926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-8453652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772048-8513281
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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 |
Jun
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
308 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
607-12
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1995
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pubmed:articleTitle |
Localization of Ca(2+)-dependent conformational changes of calretinin by limited tryptic proteolysis.
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pubmed:affiliation |
Laboratory of Clinical Science, National Institute of Mental Health, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article
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