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Article: Isolation of leptin-binding peptides from a random peptide phage library

TitleIsolation of leptin-binding peptides from a random peptide phage library
Authors
KeywordsBaculovirus
Leptin
Peptide
Phage library
Issue Date2000
PublisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/cbdd
Citation
Journal Of Peptide Research, 2000, v. 55 n. 4, p. 318-324 How to Cite?
AbstractLeptin plays a role in regulating the body weight in mice. Injection of recombinant mouse leptin expressed in Escherichia coli reduced the food intake and body weight in normal, ob/ob and diet-induced obesity mice. Hyperglycemia, hyperinsulinemia and hypothermia can also be corrected in ob/ob mice after leptin injection. Leptin is a 16-kDa secretory protein comprising 167 amino acids produced in adipose tissue and is secreted to blood stream. In this study, a recombinant mouse leptin was generated and purified from a baculovirus expression system. This protein was used to identify putative ligands using a phage library of random peptides. Three leptin-binding phage clones were found, which were characterized by DNA sequencing and ELISA methods. The amino acid sequences of the reactive peptides are: LAYCSDPVRCLVWWY, MFWlSAVSFVDHALV and LVLVLSAFLCCGVG. All three clones bound to recombinant human and mouse leptins. These peptides may be useful tools to study leptin-receptor interaction, food intake and body weight regulation.
Persistent Identifierhttp://hdl.handle.net/10722/54341
ISSN
2007 Impact Factor: 1.303
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, KWen_HK
dc.contributor.authorLim, PLen_HK
dc.contributor.authorTam, FCHen_HK
dc.contributor.authorLi, ETSen_HK
dc.contributor.authorLim, BLen_HK
dc.date.accessioned2009-04-03T07:43:52Z-
dc.date.available2009-04-03T07:43:52Z-
dc.date.issued2000en_HK
dc.identifier.citationJournal Of Peptide Research, 2000, v. 55 n. 4, p. 318-324en_HK
dc.identifier.issn1397-002Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/54341-
dc.description.abstractLeptin plays a role in regulating the body weight in mice. Injection of recombinant mouse leptin expressed in Escherichia coli reduced the food intake and body weight in normal, ob/ob and diet-induced obesity mice. Hyperglycemia, hyperinsulinemia and hypothermia can also be corrected in ob/ob mice after leptin injection. Leptin is a 16-kDa secretory protein comprising 167 amino acids produced in adipose tissue and is secreted to blood stream. In this study, a recombinant mouse leptin was generated and purified from a baculovirus expression system. This protein was used to identify putative ligands using a phage library of random peptides. Three leptin-binding phage clones were found, which were characterized by DNA sequencing and ELISA methods. The amino acid sequences of the reactive peptides are: LAYCSDPVRCLVWWY, MFWlSAVSFVDHALV and LVLVLSAFLCCGVG. All three clones bound to recombinant human and mouse leptins. These peptides may be useful tools to study leptin-receptor interaction, food intake and body weight regulation.en_HK
dc.languageengen_HK
dc.publisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/cbdden_HK
dc.relation.ispartofJournal of Peptide Researchen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsThe definitive version is available at www.blackwell-synergy.comen_HK
dc.subjectBaculovirusen_HK
dc.subjectLeptinen_HK
dc.subjectPeptideen_HK
dc.subjectPhage libraryen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshBacteriophages - metabolismen_HK
dc.subject.meshBaculoviridae - geneticsen_HK
dc.subject.meshEnzyme-Linked Immunosorbent Assayen_HK
dc.subject.meshEscherichia coli - genetics - metabolismen_HK
dc.titleIsolation of leptin-binding peptides from a random peptide phage libraryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1397-002X&volume=55&issue=4&spage=318&epage=324&date=2000&atitle=Isolation+of+leptin-binding+peptides+from+a+random+peptide+phage+libraryen_HK
dc.identifier.emailLi, ETS: etsli@hku.hken_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityLi, ETS=rp00737en_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1034/j.1399-3011.2000.00679.xen_HK
dc.identifier.pmid10798377-
dc.identifier.scopuseid_2-s2.0-0034036696en_HK
dc.identifier.hkuros48426-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034036696&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume55en_HK
dc.identifier.issue4en_HK
dc.identifier.spage318en_HK
dc.identifier.epage324en_HK
dc.identifier.isiWOS:000086498500007-
dc.publisher.placeDenmarken_HK
dc.identifier.scopusauthoridChan, KW=8587755300en_HK
dc.identifier.scopusauthoridLim, PL=7202592401en_HK
dc.identifier.scopusauthoridTam, FCH=7004921628en_HK
dc.identifier.scopusauthoridLi, ETS=14018169600en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK

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