DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, JH | ko |
dc.contributor.author | Park, CB | ko |
dc.contributor.author | Yoon, YG | ko |
dc.contributor.author | Kim, Sun-Chang | ko |
dc.date.accessioned | 2013-03-03T06:59:03Z | - |
dc.date.available | 2013-03-03T06:59:03Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1998-10 | - |
dc.identifier.citation | BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE, v.1408, no.1, pp.67 - 76 | - |
dc.identifier.issn | 0925-4439 | - |
dc.identifier.uri | http://hdl.handle.net/10203/77703 | - |
dc.description.abstract | A novel antimicrobial peptide was isolated and characterized from the earthworm, Lumbricus rubellus. The antimicrobial peptide was purified to homogeneity by a heparin-affinity column and C18 reverse-phase HPLC, and named lumbricin I. Lumbricin I was a proline-rich antimicrobial peptide of 62 amino acids (15% proline in molar ratio; molecular mass, 7231 Da), whose complete sequence was determined by a combination of peptide sequence and cDNA analysis. The peptide and cDNA sequence analysis revealed that lumbricin I was produced as a precursor form consisting of 76 amino acids, with 14 residues in a presegment and 62 residues in mature lumbricin I. Lumbricin I showed antimicrobial activity in vitro against a broad spectrum of microorganisms without hemolytic activity. In addition, a 29-amino acid peptide, named lumbricin I(6-34), which was derived from residues 6-34 of lumbricin I, showed marginally stronger antimicrobial activity than lumbricin I. Northern blot analysis on total RNA revealed that expression of lumbricin I gene was not induced by bacterial infection, but was constitutively expressed. Furthermore, the expression of lumbricin I gene was specific in adult L. rubellus: Lumbricin I mRNA was detected only in adult L, rubellus, but not in eggs and young L. rubellus. (C) 1998 Elsevier Science B.V. All rights reserved. | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | EISENIA-FETIDA-ANDREI | - |
dc.subject | ANTIBACTERIAL PEPTIDES | - |
dc.subject | CELOMIC FLUID | - |
dc.subject | PIG INTESTINE | - |
dc.subject | ANTIBIOTICS | - |
dc.subject | SEQUENCE | - |
dc.subject | PROTEINS | - |
dc.subject | SYSTEM | - |
dc.subject | PR-39 | - |
dc.subject | BACTENECINS | - |
dc.title | Lumbricin I, a novel proline-rich antimicrobial peptide from the earthworm: purification, cDNA cloning and molecular characterization | - |
dc.type | Article | - |
dc.identifier.wosid | 000076723700007 | - |
dc.identifier.scopusid | 2-s2.0-0031762466 | - |
dc.type.rims | ART | - |
dc.citation.volume | 1408 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 67 | - |
dc.citation.endingpage | 76 | - |
dc.citation.publicationname | BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | - |
dc.contributor.localauthor | Kim, Sun-Chang | - |
dc.contributor.nonIdAuthor | Cho, JH | - |
dc.contributor.nonIdAuthor | Park, CB | - |
dc.contributor.nonIdAuthor | Yoon, YG | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | antimicrobial peptide | - |
dc.subject.keywordAuthor | proline-rich peptide | - |
dc.subject.keywordAuthor | earthworm | - |
dc.subject.keywordAuthor | Lumbricus rubellus | - |
dc.subject.keywordAuthor | cDNA cloning | - |
dc.subject.keywordPlus | EISENIA-FETIDA-ANDREI | - |
dc.subject.keywordPlus | ANTIBACTERIAL PEPTIDES | - |
dc.subject.keywordPlus | CELOMIC FLUID | - |
dc.subject.keywordPlus | PIG INTESTINE | - |
dc.subject.keywordPlus | ANTIBIOTICS | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | PR-39 | - |
dc.subject.keywordPlus | BACTENECINS | - |
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