Labelled 14β-cholest-5-en-3β-ol (14β-[3H]-cholesterol) was synthesized. No conversion into cholesterol was observed by incubation of this sterol with rat liver enzymes. Plasma decay rate, biliary excretion and binding to lipoproteins did not differ from those of the natural stereoisomer. However, significantly different Lecithin Cholesterol Acyl Transferase (LCAT) activity in plasma was observed when 14β-cholesterol was compared with cholesterol

Esterification, lipoprotein binding and excretion of the 14β-stereoisomer of cholesterol / M. Kienle Galli, G. Cighetti, M. Anastasia, C.R. Sirtori. - In: JOURNAL OF STEROID BIOCHEMISTRY. - ISSN 0022-4731. - 9:2(1978), pp. 127-130.

Esterification, lipoprotein binding and excretion of the 14β-stereoisomer of cholesterol

G. Cighetti
Secondo
;
M. Anastasia
Penultimo
;
C.R. Sirtori
Ultimo
1978

Abstract

Labelled 14β-cholest-5-en-3β-ol (14β-[3H]-cholesterol) was synthesized. No conversion into cholesterol was observed by incubation of this sterol with rat liver enzymes. Plasma decay rate, biliary excretion and binding to lipoproteins did not differ from those of the natural stereoisomer. However, significantly different Lecithin Cholesterol Acyl Transferase (LCAT) activity in plasma was observed when 14β-cholesterol was compared with cholesterol
liver enzyme ; phosphatidylcholine sterol acyltransferase ; 14beta cholesterol ; isomerism ; methodology ; rat, Animal ; Lipoproteins ; Phosphatidylcholine-Sterol O-Acyltransferase
Settore BIO/10 - Biochimica
Settore BIO/14 - Farmacologia
1978
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/185439
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