Literature DB >> 3932371

Interaction of very low density lipoprotein with chicken oocyte membranes.

S A Krumins, T F Roth.   

Abstract

The interaction of hen 125I-VLDL (very low density lipoprotein) with chicken oocyte membranes was characterized using a rapid sedimentation assay. Equilibrium and kinetic studies showed an apparent dissociation constant (Kd) 8.7-9.1 x 10(-8) M or 43.5-45.5 micrograms VLDL protein/ml. Binding capacity was 2.0 micrograms VLDL protein/mg membrane homogenate protein. The apparent rate constants were k1 = 2.4 x 10(5) M-1 min-1 and k2 = 2.1 x 10(-2) min-1. Specific binding required the presence of divalent cations. Whereas binding was completely restored after treatment with EDTA by the addition of MN++, only 60% of binding was restored using Ca++.

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Year:  1985        PMID: 3932371     DOI: 10.1002/jcb.240280406

Source DB:  PubMed          Journal:  J Cell Biochem        ISSN: 0730-2312            Impact factor:   4.429


  2 in total

1.  Solubilization and characterization of the chicken oocyte vitellogenin receptor.

Authors:  S Stifani; R George; W J Schneider
Journal:  Biochem J       Date:  1988-03-01       Impact factor: 3.857

2.  Specific postendocytic proteolysis of apolipoprotein B in oocytes does not abolish receptor recognition.

Authors:  J Nimpf; M Radosavljevic; W J Schneider
Journal:  Proc Natl Acad Sci U S A       Date:  1989-02       Impact factor: 11.205

  2 in total

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