File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Identification and characterization of human serum alpha2-HS glycoprotein as a jacalin-bound protein

TitleIdentification and characterization of human serum alpha2-HS glycoprotein as a jacalin-bound protein
Authors
Keywordsα2-HS glycoprotein
Human
Jacalin
Issue Date1995
Citation
Biochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1995, v. 1249 n. 1, p. 58-64 How to Cite?
AbstractWe recently adopted immobilized jacalin as an affinity adsorbent to purify human serum IgA for laboratory study. In the course of our investigation, we detected a serum protein that co-eluted with IgA from jacalin-agarose affinity column. It constituted in significant quantity (24.0 ± 0.9%, n = 30) of total jacalin-bound protein (JBP) and the yield was equivalent to 0.4 ± 0.1 mg per ml serum. The molecular mass of this protein was 55 kDa with electromobility in the α2 region as demonstrated by SDS-PAGE and immunoelectrophoresis. N-terminal microsequencing of this 55 kDa protein revealed that it is human alpha2-HS glycoprotein (α2HSG). The molecular interaction of α2HSG with jacalin was characterized by competitive ELISA: human serum IgA, human colostrum secretory IgA (sIgA), and monosaccharides including D-galactose and melibiose exhibited strong inhibitory effect on its binding to jacalin. Accordingly, we propose that human α2HSG binds in a similar manner as that of the bovine fetuin to jacalin. In addition, α2HSG displays similar binding property to jacalin from different geographic area (India and Malaysia) and from different laboratory preparations (Sigma, Pierce and 'homemade' jacalin).
Persistent Identifierhttp://hdl.handle.net/10722/162091
ISSN
2004 Impact Factor: 3.079
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTo, WYen_HK
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorLai, KNen_HK
dc.date.accessioned2012-09-05T05:17:14Z-
dc.date.available2012-09-05T05:17:14Z-
dc.date.issued1995en_HK
dc.identifier.citationBiochimica Et Biophysica Acta - Protein Structure And Molecular Enzymology, 1995, v. 1249 n. 1, p. 58-64en_HK
dc.identifier.issn0167-4838en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162091-
dc.description.abstractWe recently adopted immobilized jacalin as an affinity adsorbent to purify human serum IgA for laboratory study. In the course of our investigation, we detected a serum protein that co-eluted with IgA from jacalin-agarose affinity column. It constituted in significant quantity (24.0 ± 0.9%, n = 30) of total jacalin-bound protein (JBP) and the yield was equivalent to 0.4 ± 0.1 mg per ml serum. The molecular mass of this protein was 55 kDa with electromobility in the α2 region as demonstrated by SDS-PAGE and immunoelectrophoresis. N-terminal microsequencing of this 55 kDa protein revealed that it is human alpha2-HS glycoprotein (α2HSG). The molecular interaction of α2HSG with jacalin was characterized by competitive ELISA: human serum IgA, human colostrum secretory IgA (sIgA), and monosaccharides including D-galactose and melibiose exhibited strong inhibitory effect on its binding to jacalin. Accordingly, we propose that human α2HSG binds in a similar manner as that of the bovine fetuin to jacalin. In addition, α2HSG displays similar binding property to jacalin from different geographic area (India and Malaysia) and from different laboratory preparations (Sigma, Pierce and 'homemade' jacalin).en_HK
dc.languageengen_US
dc.relation.ispartofBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymologyen_HK
dc.subjectα2-HS glycoproteinen_HK
dc.subjectHumanen_HK
dc.subjectJacalinen_HK
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBlood Proteins - Chemistry - Isolation & Purificationen_US
dc.subject.meshChromatography, Affinityen_US
dc.subject.meshHumansen_US
dc.subject.meshImmunoglobulin A - Chemistry - Isolation & Purificationen_US
dc.subject.meshLectins - Chemistryen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPlant Lectinsen_US
dc.subject.meshAlpha-2-Hs-Glycoproteinen_US
dc.titleIdentification and characterization of human serum alpha2-HS glycoprotein as a jacalin-bound proteinen_HK
dc.typeArticleen_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.emailLai, KN: knlai@hku.hken_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.identifier.authorityLai, KN=rp00324en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0167-4838(95)00063-Zen_HK
dc.identifier.pmid7766684-
dc.identifier.scopuseid_2-s2.0-0029044588en_HK
dc.identifier.volume1249en_HK
dc.identifier.issue1en_HK
dc.identifier.spage58en_HK
dc.identifier.epage64en_HK
dc.identifier.isiWOS:A1995RA12000007-
dc.identifier.scopusauthoridTo, WY=36933508500en_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats