Literature DB >> 7248326

Affinity chromatography of arterial lysosomal cholesterol ester hydrolase.

J C Dousset, N Dousset, M J Foglietti, L Douste-Blazy.   

Abstract

The glycoproteic nature of rabbit aortic lysosomal cholesterol ester hydrolase has been demonstrated by affinity chromatography on Concanavalin A-Sepharose. After chromatography, the enzyme lacks synthesizing activity. This activity is restored by addition of deactivated lysosomes containing more endogenous cholesterol. On the other hand, a hypothesis for the activation role of bis(monoacylglyceryl) phosphate is suggested.

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Year:  1981        PMID: 7248326     DOI: 10.1016/0005-2760(81)90050-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  Cupric ion-dependent inhibition of lysosomal acid cholesteryl ester hydrolase in the presence of hydroxylamine.

Authors:  M Tanaka; T Iio; T Tabata
Journal:  Lipids       Date:  1988-02       Impact factor: 1.880

2.  Characterization of a cytosolic protein inhibiting lysosomal acid cholesteryl ester hydrolase.

Authors:  M Tanaka; R Yonekura; T Iio; T Tabata
Journal:  Lipids       Date:  1984-10       Impact factor: 1.880

3.  Properties of an acid cholesteryl ester hydrolase inhibitor from rat serum.

Authors:  M Tanaka; T Iio; T Tabata
Journal:  Lipids       Date:  1990-12       Impact factor: 1.880

4.  Effect of cupric ions on serum and liver cholesterol metabolism.

Authors:  M Tanaka; T Iio; T Tabata
Journal:  Lipids       Date:  1987-12       Impact factor: 1.880

  4 in total

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