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Article: APF/CBP, the small, amphipathic, anionic protein(s) in bile and gallstones, consists of lipid-binding and calcium-binding forms

TitleAPF/CBP, the small, amphipathic, anionic protein(s) in bile and gallstones, consists of lipid-binding and calcium-binding forms
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1997
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.hepatology.org/
Citation
Hepatology, 1997, v. 25 n. 5, p. 1054-1063 How to Cite?
AbstractTwo very similar small anionic, amphipathic proteins, a phospholipid- binding apoprotein (anionic polypeptide fraction [APF]) and a calcium- binding polypeptide (CBP), are found abundantly in bile and all types of gallstones. The often disparate properties among various preparations of APF/CBP could reflect different sources and separation procedures, leading to partly degraded and/or denatured protein and varied association of bile salts, lipids, bile pigments, and detergents. The present study presents new methods for isolation and purification of APF/CBP, and characterizes the preparations thus obtained. It was found that isolation by selective precipitation of proteins from fresh T-tube bile by added calcium chloride, followed by demineralization with ethylenediaminetetraacetic acid (EDTA), removal of salts, lipids, and some pigment by Sephadex LH-20, and serial ultrafiltration yields the purest preparations. Though free of lipids, bile salts, detergents, and most pigments, these new preparations all show the same 7-kd and 12-kd bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the same major peaks on hydrophobic high- performance liquid chromatography (HPLC), and retain the self-associative, lipid- and calcium-binding functions, typical of older preparations obtained by potentially denaturative procedures. The varied properties among APF/CBP preparations are thus apparently related mainly to their content of different proportions of two major components, lipid-binding APF and calcium-binding CBP. Immunologic cross-reactions indicate common epitopes, and amino acid analyses are also similar, suggesting that APF and CBP may have the same polypeptide backbone, but differ because of posttranslational modification(s). Sufficiently pure APF and CBP have now been obtained to permit possible structural identification by sequencing and molecular biological techniques, though such attempts have thus far been unsuccessful.
Persistent Identifierhttp://hdl.handle.net/10722/92517
ISSN
2015 Impact Factor: 11.711
2015 SCImago Journal Rankings: 4.752
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLafont, Hen_HK
dc.contributor.authorDomingo, Nen_HK
dc.contributor.authorGroen, Aen_HK
dc.contributor.authorKaler, EWen_HK
dc.contributor.authorLee, SPen_HK
dc.contributor.authorKoehler, Ren_HK
dc.contributor.authorOstrow, JDen_HK
dc.contributor.authorVeis, Aen_HK
dc.date.accessioned2010-09-17T10:48:39Z-
dc.date.available2010-09-17T10:48:39Z-
dc.date.issued1997en_HK
dc.identifier.citationHepatology, 1997, v. 25 n. 5, p. 1054-1063en_HK
dc.identifier.issn0270-9139en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92517-
dc.description.abstractTwo very similar small anionic, amphipathic proteins, a phospholipid- binding apoprotein (anionic polypeptide fraction [APF]) and a calcium- binding polypeptide (CBP), are found abundantly in bile and all types of gallstones. The often disparate properties among various preparations of APF/CBP could reflect different sources and separation procedures, leading to partly degraded and/or denatured protein and varied association of bile salts, lipids, bile pigments, and detergents. The present study presents new methods for isolation and purification of APF/CBP, and characterizes the preparations thus obtained. It was found that isolation by selective precipitation of proteins from fresh T-tube bile by added calcium chloride, followed by demineralization with ethylenediaminetetraacetic acid (EDTA), removal of salts, lipids, and some pigment by Sephadex LH-20, and serial ultrafiltration yields the purest preparations. Though free of lipids, bile salts, detergents, and most pigments, these new preparations all show the same 7-kd and 12-kd bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the same major peaks on hydrophobic high- performance liquid chromatography (HPLC), and retain the self-associative, lipid- and calcium-binding functions, typical of older preparations obtained by potentially denaturative procedures. The varied properties among APF/CBP preparations are thus apparently related mainly to their content of different proportions of two major components, lipid-binding APF and calcium-binding CBP. Immunologic cross-reactions indicate common epitopes, and amino acid analyses are also similar, suggesting that APF and CBP may have the same polypeptide backbone, but differ because of posttranslational modification(s). Sufficiently pure APF and CBP have now been obtained to permit possible structural identification by sequencing and molecular biological techniques, though such attempts have thus far been unsuccessful.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.hepatology.org/en_HK
dc.relation.ispartofHepatologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.titleAPF/CBP, the small, amphipathic, anionic protein(s) in bile and gallstones, consists of lipid-binding and calcium-binding formsen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, SP: sumlee@hku.hken_HK
dc.identifier.authorityLee, SP=rp01351en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid9141417-
dc.identifier.scopuseid_2-s2.0-0031007718en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031007718&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume25en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1054en_HK
dc.identifier.epage1063en_HK
dc.identifier.isiWOS:A1997WX60400003-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLafont, H=24289428600en_HK
dc.identifier.scopusauthoridDomingo, N=7004865212en_HK
dc.identifier.scopusauthoridGroen, A=35242574800en_HK
dc.identifier.scopusauthoridKaler, EW=7007157989en_HK
dc.identifier.scopusauthoridLee, SP=7601417497en_HK
dc.identifier.scopusauthoridKoehler, R=7102067978en_HK
dc.identifier.scopusauthoridOstrow, JD=7005838021en_HK
dc.identifier.scopusauthoridVeis, A=7101829537en_HK

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