Literature DB >> 6789904

Evaluation of the mixed interaction between apolipoproteins A-II and C-I equilibrium sedimentation.

L Servillo, H B Brewer, J C Osborne.   

Abstract

The mixed interaction between human apolipoproteins C-I and A-II, each of which self-associate is aqueous solution, has been evaluated by sedimentation equilibrium measurements. In order to simplify data analysis apoC-I and apoA-II were modified by treatment with 2-nitrophenylsulfenyl chloride and tetranitromethane respectively. The molecular properties of the resulting derivatives, S-apoC-I and N-apo-A-II, each of which appreciable extinction coefficients above 350 nm, were indistinguishable from the corresponding unmodified species. Sedimentation equilibrium data were obtained with mixtures of S-apoC-I and native apoA-II, N-apoA-II and native apoC-I, and native apoC-I and native apoA-II. Mixed complex formation was detected readily with all mixtures investigated. The combined results were most consistent with a single mixed oligomer containing 2 molecules of apoA-II and 4 molecules of apoC-I. The corresponding equilibrium constant was 31248 +/- 890 (l/gm)5.

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Year:  1981        PMID: 6789904     DOI: 10.1016/0301-4622(81)80022-1

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  1 in total

1.  Studying multiprotein complexes by multisignal sedimentation velocity analytical ultracentrifugation.

Authors:  Andrea Balbo; Kenneth H Minor; Carlos A Velikovsky; Roy A Mariuzza; Cynthia B Peterson; Peter Schuck
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-21       Impact factor: 11.205

  1 in total

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