On the tracks of our scientific forbears.
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Biomedical subjects
Publications and source records attributed to F Schlenk.
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5'-Methylthio[U-14C]adenosine was used as a culture supplement for Candida utilis. The resulting S-adenosylmethionine was hydrolyzed into its structural components. Virtually none of the label of the pentose was found in the carbohydrate part of the intracellular S-adenosylmethionine. Much of it was present in the four-carbon chain of the methionine part of the sulfonium compound. The (U-14C)-labeled adenine of 5'-methylthio[U-14C]adenosine did not contribute to the labeling of the amino acid components of the sulfonium compound.
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A special strain of Saccharomyces cerevisiae responded to a supplement of S-n-propyl-L-homocysteine in the culture medium by synthesizing S-adenosyl-(S-n-propyl)L-homocysteine, the S-n-propyl analogue of S-adenosylmethionine. S-n-Butyl-L-homocysteine reacted sparingly with this strain, but S-isopropyl-L-homocysteine failed to form detectable quantities of the corresponding S-adenosylsulfonium compound. The S-n-propyl compound was isolated by extraction of the cells, followed by ion-exchange chromatography, which separated it from endogenous S-adenosylmethionine. The structure was determined by hydrolytic procedures leading to overlapping fragments of known structure, 5'-n-propylthioadenosine and S-n-propyl-L-homocysteine. The new sulfonium compound was examined for its activity as n-propyl donor by substituting it for S-adenosylmethionine in methyltransferase systems. Enzymatic transpropylation was observed with S-adenosylmethionine : L-homocysteine S-methyltransferase (EC 2.1.1.10). Its rate was low in the S-adenosylmethionine : N-acetylserotonin O-methyltransferase system (EC 2.1.1.4), and below recognition with S-adenosylmethionine : guanidinoacetate methyltransferase (EC 2.1.1.2) and S-adenosylmethionine : histamine N-methyltransferase (EC 2.1.1.8).
Isolated vacuoles of the yeast Candida utilis did not show active transport of S-adenosylmethionine, uric acid, and several amino acids which they concentrate in vivo.
Saccharomyces cerevisiae 4094-B (alpha, ade-2, ura-1) in potassium phosphate buffer with glucose under aerobic conditions took up (-)S-adenosyl-l-methionine from the medium in sufficient quantity to permit the demonstration of its accumulation in the vacuole by ultraviolet micrography. The same result was obtained with (+/-)S-adenosyl-l-methionine, (+/-)S-adenosyl-d-methionine, and (-)S-adenosyl-l-ethionine. The rate of uptake was slow with (-)S-adenosyl-S(n-propyl)-l-homocysteine and S-adenosyl-d-homocysteine. S-Adenosyl-l-homocysteine was assimilated rapidly, but intracellular degradation precluded accumulation and ultraviolet micrographic studies. The uptake of 5'-methyl-, 5'-ethyl-, 5'-n-propylthioadenosine, and 5'-dimethylsulfonium adenosine was minimal.
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Candida utilis cells and spheroplasts containing uric acid crystals in their vacuoles were not damaged by the mechanical stress of centrifugation at 20,000 x g for 10 min, as judged by plating, microscopy, and spectrophotometry.
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