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Article: Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin

TitleStructural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin
Authors
Issue Date1993
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/IMM
Citation
Immunology, 1993, v. 78 n. 1, p. 159-165 How to Cite?
AbstractConglutinin is a Ca2+-dependent, carbohydrate-binding, serum protein which contains an N-terminal collagen-like region and a C-terminal, C-type lectin domain. To date, conglutinin, which appears to play an important role in defence mechanisms, has been fully described, by protein sequence analysis, only in the bovine system. To allow comparison of lung surfactant protein D (SP-D) with conglutinin, within one species, a full-length cDNA clone for SP-D has been isolated from a bovine lung library. The derived amino acid sequence for bovine SP-D shows a higher (78%) level of identity to the sequence of conglutinin than to the sequence of human or rat SP-D (67 and 65% respectively). However, SP-D and conglutinin are known to have different carbohydrate-binding specificities, therefore some of the 16 residues conserved in the C-type lectin domains of all three species of SP-D, but which are not conserved in conglutinin, appear likely to be involved in determination of specificity. The use of a polymerase chain reaction (PCR)-derived DNA probe for bovine SP-D in Northern blotting studies yielded a signal from bovine liver mRNA as well as the expected signal from bovine lung mRNA. Since SP-D appears to be a lung-specific protein, it seems probable that the liver is the primary site of synthesis of conglutinin.
Persistent Identifierhttp://hdl.handle.net/10722/178551
ISSN
2015 Impact Factor: 4.078
2015 SCImago Journal Rankings: 2.038
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLim, BLen_US
dc.contributor.authorLu, Jen_US
dc.contributor.authorReid, KBMen_US
dc.date.accessioned2012-12-19T09:48:20Z-
dc.date.available2012-12-19T09:48:20Z-
dc.date.issued1993en_US
dc.identifier.citationImmunology, 1993, v. 78 n. 1, p. 159-165en_US
dc.identifier.issn0019-2805en_US
dc.identifier.urihttp://hdl.handle.net/10722/178551-
dc.description.abstractConglutinin is a Ca2+-dependent, carbohydrate-binding, serum protein which contains an N-terminal collagen-like region and a C-terminal, C-type lectin domain. To date, conglutinin, which appears to play an important role in defence mechanisms, has been fully described, by protein sequence analysis, only in the bovine system. To allow comparison of lung surfactant protein D (SP-D) with conglutinin, within one species, a full-length cDNA clone for SP-D has been isolated from a bovine lung library. The derived amino acid sequence for bovine SP-D shows a higher (78%) level of identity to the sequence of conglutinin than to the sequence of human or rat SP-D (67 and 65% respectively). However, SP-D and conglutinin are known to have different carbohydrate-binding specificities, therefore some of the 16 residues conserved in the C-type lectin domains of all three species of SP-D, but which are not conserved in conglutinin, appear likely to be involved in determination of specificity. The use of a polymerase chain reaction (PCR)-derived DNA probe for bovine SP-D in Northern blotting studies yielded a signal from bovine liver mRNA as well as the expected signal from bovine lung mRNA. Since SP-D appears to be a lung-specific protein, it seems probable that the liver is the primary site of synthesis of conglutinin.en_US
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/IMMen_US
dc.relation.ispartofImmunologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBlotting, Northernen_US
dc.subject.meshCattleen_US
dc.subject.meshCollectinsen_US
dc.subject.meshDna - Chemistryen_US
dc.subject.meshGlycoproteins - Chemistry - Geneticsen_US
dc.subject.meshLiver - Metabolismen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPolymerase Chain Reactionen_US
dc.subject.meshPulmonary Surfactant-Associated Protein Den_US
dc.subject.meshPulmonary Surfactants - Chemistry - Geneticsen_US
dc.subject.meshSerum Globulins - Biosynthesis - Chemistryen_US
dc.titleStructural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutininen_US
dc.typeArticleen_US
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_US
dc.identifier.authorityLim, BL=rp00744en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid8436402-
dc.identifier.scopuseid_2-s2.0-0027459854en_US
dc.identifier.volume78en_US
dc.identifier.issue1en_US
dc.identifier.spage159en_US
dc.identifier.epage165en_US
dc.identifier.isiWOS:A1993KH15500024-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridLim, BL=7201983917en_US
dc.identifier.scopusauthoridLu, J=7601564408en_US
dc.identifier.scopusauthoridReid, KBM=7202780648en_US

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