Matches in SemOpenAlex for { <https://semopenalex.org/work/W1569494614> ?p ?o ?g. }
Showing items 1 to 79 of
79
with 100 items per page.
- W1569494614 endingPage "57" @default.
- W1569494614 startingPage "47" @default.
- W1569494614 abstract "Fractionation of the three main genetic variants (F1, S and A) of human alpha 1-acid glycoprotein (AAG), in their native (sialylated) form, by chromatography on immobilized copper(II) affinity adsorbent was investigated. This chromatographic method had been previously developed to fractionate the desialylated protein variants. For that purpose, the three main AAG phenotypes samples (F1S/A, F1/A and S/A), which had been previously isolated from individual human plasma samples, and an AAG sample from commercial source (a mixture of the phenotypes) were used in the native form. Affinity chromatography of these different samples on an iminodiacetate Sepharose-copper(II) gel at pH 7 resolved two protein peaks, irrespective of the origin of the native AAG sample used. The unbound peak 1 was found to consist of the F1, the S or both variants, depending on the phenotype of the AAG sample used in the chromatography. The bound peak 2 was found to consist of the A variant in a pure form. The fractionation results obtained with native AAG were found to be the same as those originally yielded by the desialylated protein. However, comparison of the interactions of native and desialylated AAG with immobilized copper(II) ions, using an affinity chromatographic method and a non-chromatographic equilibrium binding technique, respectively, showed that desialylation increased the non-specific interactions of the protein with immobilized copper(II) ions. The AAG variants were not fractionated when affinity chromatography was performed using immobilized zinc, nickel or cobalt(II) ions, instead of copper. After purification of each variant in the sialylated form (F1, S and A), their respective heterogeneity was studied by analytical isoelectrofocusing with carrier ampholytes in the pH range 2.5-4.5. In addition, the lectin-binding behaviour of the separate sialylated AAG variants was investigated by affinity chromatography on immobilized concanavalin A." @default.
- W1569494614 created "2016-06-24" @default.
- W1569494614 creator A5021085069 @default.
- W1569494614 creator A5045782776 @default.
- W1569494614 creator A5046268899 @default.
- W1569494614 creator A5090672798 @default.
- W1569494614 date "1993-05-19" @default.
- W1569494614 modified "2023-09-30" @default.
- W1569494614 title "Fractionation of the genetic variants of human alpha 1-acid glycoprotein in the native form by chromatography on an immobilized copper(II) affinity adsorbent. Heterogeneity of the separate variants by isoelectrofocusing and by concanavalin A affinity chromatography." @default.
- W1569494614 cites W1506592546 @default.
- W1569494614 cites W163526048 @default.
- W1569494614 cites W2025777047 @default.
- W1569494614 cites W2027637212 @default.
- W1569494614 cites W2067574677 @default.
- W1569494614 cites W2076832468 @default.
- W1569494614 cites W2081639720 @default.
- W1569494614 cites W2084037895 @default.
- W1569494614 cites W2095500488 @default.
- W1569494614 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8340462" @default.
- W1569494614 hasPublicationYear "1993" @default.
- W1569494614 type Work @default.
- W1569494614 sameAs 1569494614 @default.
- W1569494614 citedByCount "8" @default.
- W1569494614 countsByYear W15694946142019 @default.
- W1569494614 countsByYear W15694946142023 @default.
- W1569494614 crossrefType "journal-article" @default.
- W1569494614 hasAuthorship W1569494614A5021085069 @default.
- W1569494614 hasAuthorship W1569494614A5045782776 @default.
- W1569494614 hasAuthorship W1569494614A5046268899 @default.
- W1569494614 hasAuthorship W1569494614A5090672798 @default.
- W1569494614 hasConcept C108625454 @default.
- W1569494614 hasConcept C116817701 @default.
- W1569494614 hasConcept C150394285 @default.
- W1569494614 hasConcept C178790620 @default.
- W1569494614 hasConcept C179247698 @default.
- W1569494614 hasConcept C179998833 @default.
- W1569494614 hasConcept C181199279 @default.
- W1569494614 hasConcept C185592680 @default.
- W1569494614 hasConcept C2779881004 @default.
- W1569494614 hasConcept C43617362 @default.
- W1569494614 hasConcept C544778455 @default.
- W1569494614 hasConcept C55493867 @default.
- W1569494614 hasConcept C73826308 @default.
- W1569494614 hasConcept C97428945 @default.
- W1569494614 hasConceptScore W1569494614C108625454 @default.
- W1569494614 hasConceptScore W1569494614C116817701 @default.
- W1569494614 hasConceptScore W1569494614C150394285 @default.
- W1569494614 hasConceptScore W1569494614C178790620 @default.
- W1569494614 hasConceptScore W1569494614C179247698 @default.
- W1569494614 hasConceptScore W1569494614C179998833 @default.
- W1569494614 hasConceptScore W1569494614C181199279 @default.
- W1569494614 hasConceptScore W1569494614C185592680 @default.
- W1569494614 hasConceptScore W1569494614C2779881004 @default.
- W1569494614 hasConceptScore W1569494614C43617362 @default.
- W1569494614 hasConceptScore W1569494614C544778455 @default.
- W1569494614 hasConceptScore W1569494614C55493867 @default.
- W1569494614 hasConceptScore W1569494614C73826308 @default.
- W1569494614 hasConceptScore W1569494614C97428945 @default.
- W1569494614 hasIssue "1" @default.
- W1569494614 hasLocation W15694946141 @default.
- W1569494614 hasOpenAccess W1569494614 @default.
- W1569494614 hasPrimaryLocation W15694946141 @default.
- W1569494614 hasRelatedWork W14949042 @default.
- W1569494614 hasRelatedWork W1544290213 @default.
- W1569494614 hasRelatedWork W1569494614 @default.
- W1569494614 hasRelatedWork W1992096985 @default.
- W1569494614 hasRelatedWork W2006642465 @default.
- W1569494614 hasRelatedWork W2015843658 @default.
- W1569494614 hasRelatedWork W2017018439 @default.
- W1569494614 hasRelatedWork W2041992805 @default.
- W1569494614 hasRelatedWork W2156604051 @default.
- W1569494614 hasRelatedWork W2368877937 @default.
- W1569494614 hasVolume "615" @default.
- W1569494614 isParatext "false" @default.
- W1569494614 isRetracted "false" @default.
- W1569494614 magId "1569494614" @default.
- W1569494614 workType "article" @default.