Abstract
ON THE MECHANISM OF ENZYMATIC CYCLIZATION OF SQUALENE
Highlights
The rat liver homogenates were prepared under the conditions for optimal formation of lanosterol described in the preceding paper [8]
In the experiment with O’*-enriched oxygen gas, the incubation was carried out in flasks designed after Thunberg t,ubes w&h 125 ml. suct,ion flasks replacing t’he tubes
Last column in Table I, the lanosterol samples contained no D in excess of the natural abundance, showing clearly that during the cyclization process there is no uptake of proton from the medium by t,he lanosterol molecule into any non-exchangeable position.’
Summary
The rat liver homogenates were prepared under the conditions for optimal formation of lanosterol described in the preceding paper [8]. A\fter aging of the homogenates for 10 minutes at room t,emperature, 2 volumes of ice-cold phosphate buffer (0.1 M, pH 7.4) in DzO were added. In the experiment with O’*-enriched oxygen gas, the incubation was carried out in flasks designed after Thunberg t,ubes w&h 125 ml. Squalene was suspended in the supernatant fluid of liver homogenate (rentrifugation for 40 minutes at 144,000 X g) and placed in the top compartment,. Analyses on a sample of the oxygen-helium mixture showed it to contain 10.9 atom per cent excess Ols. KOH and the non-saponifiable material was extracted with petroleum et,her (b.p. 30-60’). The lanosterol samples were characterized as described in the previous paper [8]
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