Document Detail

Electron-microscopic and hydrodynamic characterization of recombinant apolipoprotein (a) and its association with LDL.
MedLine Citation:
PMID:  8187249     Owner:  NLM     Status:  MEDLINE    
A recombinant apo(a) containing 17 kringle 4 domains as well as the kringle 5 and protease domains of apo(a) was characterized by hydrodynamic studies and electron microscopy. Recombinant apo(a) is a monomer in solution with a molecular weight of 325,000 by sedimentation equilibrium and 320,000 by sedimentation and diffusion, and it is a highly asymmetric molecule with a frictional ratio of 2.2. In the electron microscope recombinant apo(a) is visualized as a flexible chain of domains approximately 800 A long. Sedimentation velocity studies also demonstrate that when it is mixed with LDL, recombinant apo(a) reversibly forms an Lp(a)-like complex with a 1:1 stoichiometry; moreover, complex formation is inhibited by 6-amino hexanoic acid. Hydrodynamic modeling and electron microscopy suggest that only a small portion of the r-apo(a) molecule interacts with the LDL and the rest of the chain extends into solution. Preliminary studies indicate that recombinant apo(a) also binds mouse LDL.
M L Phillips; A V Lembertas; V N Schumaker; R M Lawn; S J Shire; T F Zioncheck
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Publication Detail:
Type:  In Vitro; Journal Article    
Journal Detail:
Title:  Chemistry and physics of lipids     Volume:  67-68     ISSN:  0009-3084     ISO Abbreviation:  Chem. Phys. Lipids     Publication Date:  1994 Jan 
Date Detail:
Created Date:  1994-06-23     Completed Date:  1994-06-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0067206     Medline TA:  Chem Phys Lipids     Country:  IRELAND    
Other Details:
Languages:  eng     Pagination:  91-7     Citation Subset:  IM    
Department of Chemistry and Biochemistry, University of California, Los Angeles 90024.
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MeSH Terms
Apolipoproteins / chemistry,  metabolism*,  ultrastructure*
Lipoproteins, LDL / metabolism*
Microscopy, Electron
Molecular Weight
Protein Binding
Protein Conformation
Recombinant Proteins / chemistry,  metabolism,  ultrastructure
Reg. No./Substance:
0/Apolipoproteins; 0/Lipoprotein(a); 0/Lipoproteins, LDL; 0/Recombinant Proteins; 0/Solutions; EC 3.4.21.-/Apoprotein(a)

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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