1951
DOI: 10.1002/hlca.19510340212
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Die Synthese des natürlichen Alliins und seiner drei optisch aktiven Isomeren. 5. Mitteilung über Allium‐Substanzen

Abstract: I n der vorhergehenden vorlaufigen Mitteilung1) haben wir iiber die Zerlegung des synthetischen, am Schwefelatom racemischen Exper. 6, 330 (1950).2) Unter ,,am Schwefelatom racemisches Alliin" verstehen wir S-Allyl-L-cysteinsulfoxyd, das in bezug a d die Konfiguration des Schwefelatoms ein Gemisch aus gleichen Teilen der rechtsdrehenden und der linksdrehenden Komponente darstellt. 5)A.

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Cited by 63 publications
(23 citation statements)
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“…First, Allicin (diallyl disulfide oxide, Figure 1) was synthesized by a modified method of Stoll and Seebeck, (1948). Allylmercaptocaptopril (AMC) was synthesized by the addition of captopril (CP) solution (1 mmol in 7.5 ml water, pH 5.5) to an aqueous solution of 0.55 mmol allicin.…”
Section: Synthesis Of Allylmercaptocaptoprilmentioning
confidence: 99%
“…First, Allicin (diallyl disulfide oxide, Figure 1) was synthesized by a modified method of Stoll and Seebeck, (1948). Allylmercaptocaptopril (AMC) was synthesized by the addition of captopril (CP) solution (1 mmol in 7.5 ml water, pH 5.5) to an aqueous solution of 0.55 mmol allicin.…”
Section: Synthesis Of Allylmercaptocaptoprilmentioning
confidence: 99%
“…1) was synthesized by a modified method of Stoll and Seebeck [9]. To a solution of diallyl disulfide (3.24 g, 0.02mol) in 15 ml of acetic acid, 30% hydrogen peroxide (5 ml) was added dropwise.…”
Section: Synthesis Of Allicinmentioning
confidence: 99%
“…This reservoir was integrated into two closed pump circuits: one contained the cartridge filled with the sample and the second circuit was connected to the flow-through cell of the photometer (flow rates: 0.5 mL/min and 2.5 mL/min, respectively). After equilibration of the system for a few minutes, enzymatic reaction was started by the addition of 20 mol alliin, which was synthesized in optically pure form according to Stoll and Seebeck (1951), Iberl et al (1990), and Koch and Keusgen (1998). Enzyme activity was traced by the decrease of NADH at 340 nm according to Schwimmer and Mazelis (1963).…”
Section: Determination Of Enzyme Activitymentioning
confidence: 99%