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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-12-1
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pubmed:abstractText |
Antistasin is a 119 amino acid protein with anticoagulant, antimetastatic and heparin-binding properties derived from the salivary glands of the leech Haementaria officinalis (1). This protein contains a specific consensus sequence for heparin binding at its carboxyl terminal end and a region between residues 32 and 48 putatively involved in glycosaminoglycan interactions. The cyclic peptide antistasin 37-48 (C-P-H-G-F-Q-R-S-R-Y-G-C) and the carboxyl terminal fragment [A103,106,108] antistasin 93-119 (P-N-G-L-K-R-D-K-L-G-A-E-Y-A-E-A-R-P-K-R-K-L-I-P-R-L-S) were synthesized by solid-phase peptide chemistry and their interactions with 125I-labeled heparin were investigated. Heparin binding to [A103,106,108] antistasin 93-119 was specific and saturable as binding was blocked by addition of the unlabeled glycosaminoglycan. The rank order of potency of various glycosaminoglycans in blocking 125I-labeled heparin binding to [A103,106,108] antistasin 93-119 was dextran sulfate greater than heparin much greater than dermatan sulfate greater than or equal to chondroitin sulfate A and C indicating a specificity of the peptide for the glycosaminoglycan structure. Moreover, heparin binding increased linearly with increasing salt and was optimal at 0.15 M NaCl and physiological pH. In contrast, binding of heparin to the basic peptide antistasin 37-48 decreased linearly as the ionic strength of the medium was increased to physiological concentration (0.15 M) thus showing a greater specificity of heparin for [A103,106,108] antistasin 93-119. These studies indicate that residues 93-119 of antistasin mediate this inhibitor's interaction with heparin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Invertebrate Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Salivary Proteins and Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/antistasin,
http://linkedlifedata.com/resource/pubmed/chemical/ghilanten
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pubmed:status |
MEDLINE
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pubmed:issn |
0065-2598
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
313
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
135-40
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1359737-Amino Acid Sequence,
pubmed-meshheading:1359737-Animals,
pubmed-meshheading:1359737-Binding Sites,
pubmed-meshheading:1359737-Heparin,
pubmed-meshheading:1359737-Invertebrate Hormones,
pubmed-meshheading:1359737-Leeches,
pubmed-meshheading:1359737-Molecular Sequence Data,
pubmed-meshheading:1359737-Peptide Fragments,
pubmed-meshheading:1359737-Peptides, Cyclic,
pubmed-meshheading:1359737-Polysaccharides,
pubmed-meshheading:1359737-Salivary Proteins and Peptides
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pubmed:year |
1992
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pubmed:articleTitle |
Heparin binding properties of the carboxyl terminal domain of [A103,106,108] antistasin 93-119.
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pubmed:affiliation |
Marion Merrell Dow Research Institute, Cincinnati, Ohio 45215.
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pubmed:publicationType |
Journal Article
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