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Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli.
The present report is concerned with the purification and properties of the enzyme 2-keto-3-deoxygluconokinase which catalyzes the phosphorylation of 2- keto- 3- deoxy-n- gluconic acid. Expand
Estimation of 3-Deoxy Sugars by Means of the Malonaldehyde–Thiobarbituric Acid Reaction
DURING the course of our investigations on the biosynthesis of 3,6-dideoxy-hexoses, found in the endotoxins of Salmonella and Escherichia1–3 and in the eggs of Parascaris equorum4, the need arose forExpand
The formation of 2-keto-3-deoxy-n-gluconic acid as the first common intermediate in the bacterial metabolism of D-glucuronic acid and n-galacturonic acid has been described in the preceding papersExpand
Conversion of Carbon-14 Dioxide to Starch Glucose during Photosynthesis by Spinach Chloroplasts
The intact spinach chloroplast free of much cytoplasic material was employed and it was proposed that either glucose was not formed by the condensation of two triose phosphates of similar tracer distribution or a pool of unlabelled dihydroxyacetone phosphate was present in the cell, causing a dilution of the upper three carbon atoms of the hexose. Expand
Metabolism of pentoses by clostridia. II. The fermentation of C14-labeled pentoses by Clostridium per fringens, Clostridium beijerinckii, and Clostridium butylicum.
The distribution of tracer in the products of the fermentation of C14-labeled pentoses by resting cells of Clostridium perfringens indicates that these organisms metabolize D-xylose and D-ribose by means of the transketolase-transaldolase sequence followed by the EMP pathway. Expand
Glycoprotein metabolism: a UDP-galactose-glycoprotein galactosyltransferase of rat serum.
Rat serum was found to contain an enzymatic activity capable of catalyzing the transfer of galactose from UDP-galactose to ovalbumin, a glycoprotein whose carbohydrate complement does not includeExpand
Glycoprotein biosynthesis. Incorporation of glycosyl groups into endogenous acceptors in a Golgi apparatus-rich fraction of liver.
A Golgi apparatus-rich fraction from rat liver was examined for the ability to mediate steps involved in the biosynthesis of glycoproteins, and it is suggested that the alkali-stable products might represent glycosaminoglycans, while the more alkala-labile products may be glycosamine-labiles. Expand
Enzymatic transfer of 14C-glucosamine from UDP-N-acetyl-14C-glucosamine to endogenous acceptors in a Golgi apparatus-rich fraction from liver.
A Golgi apparatus-rich fraction isolated from rat liver catalyzes the transfer of glucosamine from UDP-N-acetylglucosamine to endogenous protein acceptors and Digestion with pronase converts the radioactive product of this transfer into a trichloroacetic acid-soluble form. Expand
The incorporation of 14C-glucosamine from UDP-N-acetyl-14C-glucosamine into liver microsomal protein in vitro.
Abstract A particulate enzyme preparation obtained from rat liver catalyzes the transfer of glucosamine from UDP- N -acetyl- 14 C-glucosamine to endogenous protein acceptor(s). This transfer activityExpand