Abstract:
:A rat liver-specific antigen (RLSA) solubilized with the nonionic detergent non-anonyl-N-methylglucamide was purified through affinity column chromatography with a monoclonal antibody and by high-performance liquid chromatography with a hydroxylapatite column. The purified RLSA showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was determined to be 105,000 in the presence of 2-mercaptoethanol. The antigen was reactive to the Schiff reagent and contained glucosamine, but not galactosamine, indicating that the RLSA is a glycoprotein containing an asparagine-binding type of sugar chain.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Sato K,Ikeda T,Kawai F,Osada Ydoi
10.1093/oxfordjournals.jbchem.a122134subject
Has Abstractpub_date
1987-10-01 00:00:00pages
933-8issue
4eissn
0021-924Xissn
1756-2651journal_volume
102pub_type
杂志文章abstract::Human, bovine, and mouse C1q, a subcomponent of the first complement component, were purified, and both globular (GF) and collagen-like fragments (CLF) were isolated from human and bovine C1q. Antisera were produced in rabbits with these C1q or fragments, and F(ab')2 of immunoglobulin G (IgG) was purified from the ant...
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更新日期:1976-06-01 00:00:00
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更新日期:2006-04-01 00:00:00
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a130986
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更新日期:2007-07-01 00:00:00
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pub_type: 杂志文章
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更新日期:1977-02-01 00:00:00
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pub_type: 杂志文章
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更新日期:1990-11-01 00:00:00
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更新日期:1985-07-01 00:00:00