Incorporation of 3H and 14C from (6 alpha-3H)penicillin N and (10-14C,6 alpha-3H) penicillin N into deacetoxycephalosporin C.
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ABSTRACT:
SUBMITTER: Baldwin JE
PROVIDER: S-EPMC1161726 | biostudies-other | 1980 Mar
REPOSITORIES: biostudies-other
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Project description:1. Penicillin N was synthesized by coupling alpha-amino-alpha-p-nitrobenzyl-N-p-nitro-benzyloxycarbonyl-D-adipate with 6-aminopenicillanic acid benzyl ester, followed by removal of the protecting groups through hydrogenolysis. 2. alpha-Amino-alpha-p-nitrobenzyl-N-p-nitrobenzyloxycarbonyl-D-[5-14C]adipate was prepared by treating alpha-p-nitrobenzyl-N-p-nitrobenzyloxycarbonyl-D-glutamic acid with [14C]diazomethane followed by rearrangement with silver trifluoromethanesulphonate. 3. Coupling of alpha-amino-alpha-p-nitrobenzyl-N-p-nitrobenzyloxycarbonyl-D-[5-14C]adipate with 6-aminopenicillanic acid benzyl ester gave triprotected [10-14C]penicillin N. 4. 3H was introduced at C-6 of the Schiff's base derivative (10) by oxidation followed by reduction with NaB3H4. 5. The so-derived (6 alpha-3H)-labelled Schiff's base was hydrolysed to give 6-amino [6 alpha-3H]penicillanic acid benzyl ester p-toluenesulphonic acid salt, which after coupling as the free amine with alpha-amino-alpha-p-nitrobenzyl-N-pnitrobenzyloxycarbonyl-D-adipate and then hydrogenolysis, yielded [6alpha-3H]penicillin N. 6. Triprotected [10-14C]penicillin N and triprotected [6alpha-3H]penicillin N in admixture were hydrogenolysed to give [10-14C,6alpha-3H]penicillin N.
| S-EPMC1161725 | biostudies-other
Project description:Bacillus sp. 3H-10 Genome sequencing and assembly
| PRJNA606386 | ENA
Project description:1. delta-(L-alpha-Amino[4,5-3H]adipyl)-L-cysteinyl-D-[4,4-3H]valine has been synthesized from its constituent amino acids, the L-alpha-amino[4,5-3H]adipic acid being obtained by reduction with 3H2 of methyl 5-acetamido-5,5-diethoxycarbonylpent-2-enoate and subsequent decarboxylation and hydrolysis. 2. In a cell-free system prepared by lysis of protoplasts of Cephalosporium acremonium 3H was incorporated from the doubly labelled tripeptide into a compound that behaved like penicillin N or isopenicillin N. The relative specific radioactivities of the alpha-aminoadipyl and penicillamine moieties of the penicillin were the same (within experimental error) as those of the alpha-aminoadipic acid and valine residues respectively of the tripeptide. 3. The behaviour of the labelled alpha-aminoadipic acid from the penicillin to the L-amino acid oxidase of Crotalus adamanteus venom showed that it was mainly L-alpha-aminoadipic acid. 4. The results are consistent with the hypothesis that the carbon skeleton of the LLD-tripeptide is incorporated intact into the penicillin molecule and that the first product is isopenicillin N.
| S-EPMC1161777 | biostudies-other
Project description:1. Radioactivity from l-[Me-(14)C,(3)H]methionine is incorporated into phylloquinone, plastoquinone, gamma-tocopherol, alpha-tocopherol, alpha-tocopherolquinone and ubiquinone in maize shoots. 2. Comparative studies with other terpenoids (squalene and beta-carotene) and chemical degradation of selected quinones (ubiquinone and plastoquinone) established that all the radioactivity is confined to nuclear methyl substituents. 3. In ubiquinone 76% of the radioactivity is in the methoxyl groups and 24% in the ring C-methyl group. 4. Taking the phytosterols as an internal reference and accepting the atomic ratio of (14)C/(3)H transferred from l-[Me-(14)C,(3)H]methionine to the supernumerary group at C(24) to be 1:2 the ratio of all the quinones and chromanols examined approached 1:3. After allowing for the fact that for plastoquinone, gamma-tocopherol, alpha-tocopherol and alpha-tocopherolquinone one nuclear methyl group is formed from the beta-carbon of tyrosine, these results show that one nuclear C-methyl group for phylloquinone, plastoquinone and gamma-tocopherol, two nuclear methyl groups for alpha-tocopherol and alpha-tocopherolquinone and one nuclear methyl and two methoxyl groups for ubiquinone are formed by the transfer of intact methyl groups from methionine. 5. From a comparison of the incorporation of (14)C radioactivity into these compounds it would appear that the methylation reactions involved in phylloquinone and plastoquinone biosynthesis take place in the chloroplast, whereas those involved with ubiquinone biosynthesis occur else-where within the cell.
| S-EPMC1198475 | biostudies-other
Project description:The title compound, C(3)H(5)N(2) (+)·C(10)H(15)O(4)S(-), comprises two crystallographically independent ion pairs (A and B) in the asymmetric unit with slightly different conformations due to the disordered methyl groups in the anion of molecule A. Two intra-molecular C-H?O hydrogen bonds generate S(6) ring motifs. In mol-ecule A, the methyl groups are disordered over two sets of positions with a site-ocuppancy ratio of 0.547?(9):0.453?(9). Extensive inter-molecular N-H?O and C-H?O hydrogen-bonding inter-actions occur in the crystal structure which link the mol-ecules into a two-dimensional network parallel to the (100) plane.
| S-EPMC2968277 | biostudies-literature
Project description:Bacillus aquiflavi strain:3H-10 Genome sequencing and assembly
| PRJNA757941 | ENA
Project description:In BGM cells chronically infected with measles virus, although the composition of the phospholipids is unaltered, the fatty acid composition is modified. Uninfected, lytic and persistently infected cells were labelled with [3H]arachidonic acid and [14C]stearic acid and their metabolic fate analysed. No difference in the total incorporation was observed in the different systems. However, the [14C]stearic acid and [3H]arachidonic acid were incorporated up to 2-fold and 13-fold respectively greater into the neutral lipid of persistently infected compared with that of uninfected cells. Both radioactive fatty acids were specifically accumulated in the triacylglycerol and non-esterified fatty acids fractions. Lytically infected cells were similar to uninfected cells. Although there was no significant difference in the incorporation of radioactivity into the total phospholipid in either system, there was a large decrease in [3H]arachidonic acid incorporated into phosphatidylethanolamine and to a lesser extent phosphatidylcholine and phosphatidylinositol in persistently infected cells. [14C]Stearic acid incorporation was also reduced in phosphatidylcholine and phosphatidylethanolamine fractions of persistently infected cells.
| S-EPMC1152301 | biostudies-other
Project description:Copper ion dys-homeostasis is linked to neurodegenerative diseases involving amyloid formation. Even if many amyloidogenic proteins can bind copper ions as monomers, little is known about copper interactions with the resulting amyloid fibers. Here, we investigate copper interactions with α-synuclein, the amyloid-forming protein in Parkinson's disease. Copper (Cu(II)) binds tightly to monomeric α-synuclein in vitro involving the N-terminal amine and the side chain of His50. Using purified protein and biophysical methods in vitro, we reveal that copper ions are readily incorporated into the formed amyloid fibers when present at the start of aggregation reactions, and the metal ions also bind if added to pre-formed amyloids. Efficient incorporation is observed for α-synuclein variants with perturbation of either one of the high-affinity monomer copper-binding residues (i.e., N-terminus or His50) whereas a variant with both N-terminal acetylation and His50 substituted with Ala does not incorporate any copper into the amyloids. Both the morphology of the resulting α-synuclein amyloids (amyloid fiber pitch, secondary structure, proteinase sensitivity) and the copper chemical properties (redox activity, chemical potential) are altered when copper is incorporated into amyloids. We speculate that copper chelation by α-synuclein amyloids contributes to the observed copper dys-homeostasis (e.g., reduced bioavailable levels) in Parkinson's disease patients. At the same time, amyloid-copper interactions may be protective to neuronal cells as they will shield aberrantly free copper ions from promotion of toxic reactive oxygen species.
| S-EPMC10955613 | biostudies-literature
Project description:Male BALB/C mice were injected intraperitoneally with 2.5 i.u. of gonadotrophin. After the injection, increase of beta-glucuronidase activity was first observed in the microsomal fraction. By 36h 45-50% of the total homogenate activity was found in the microsomal fraction compared with 20-25% in the control microsomal fraction. From 36 to 80h not only microsomal beta-glucuronidase but also lysosomal beta-glucuronidase increased progressively. After 69h stimulation with 2.5 i.u. of gonadotrophin, d-[1-(14)C]glucosamine or l-[U-(14)C]leucine was injected intraperitoneally. After a further 3h the kidneys were homogenized and five particulate fractions were prepared by differential centrifugation. The beta-glucuronidase in the microsomal and lysosomal fractions was released respectively by ultrasonication and by freezing and thawing treatment. The enzyme was purified by organic-solvent precipitation and by sucrose-density-gradient centrifugation. The results demonstrated the incorporation of these two labels into the mouse renal beta-glucuronidase. The microsomal beta-glucuronidase was much more radioactive than the lysosomal enzyme and approx. 80% of the newly synthesized enzyme appeared in microsomes and approx. 20% of that was found in lysosomes at this period. These results suggest that the mouse renal beta-glucuronidase is a glycoprotein and that the newly synthesized enzyme is transported from endoplasmic reticulum to lysosomes.
| S-EPMC1178842 | biostudies-other
Project description:1. [2-(3)H,U-(14)C]- or [3-(3)H,U-(14)C]-Lactate was administered by infusion or bolus injection to overnight-starved rats. Tracer lactate was injected or infused through indwelling cannulas into the aorta and blood was sampled from the vena cava (A-VC mode), or it was administered into the vena cava and sampled from the aorta (V-A mode). Sampling was continued after infusion was terminated to obtain the wash-out curves for the tracer. The activities of lactate, glucose, amino acids and water were followed. 2. The kinetics of labelled lactate in the two modes differed markedly, but the kinetics of labelled glucose were much the same irrespective of mode. 3. The kinetics of (3)H-labelled lactate differed markedly from those for [U-(14)C]lactate. Isotopic steady state was attained in less than 1h of infusion of [(3)H]lactate but required over 6h for [U-(14)C]lactate. 4. (3)H from [2-(3)H]lactate labels glucose more extensive than does that from [3-(3)H]lactate. [3-(3)H]Lactate also labels plasma amino acids. The distribution of (3)H in glucose was determined. 5. Maximal radioactivity in (3)HOH in plasma is attained in less than 1min after injection. Near-maximal radioactivity in [(14)C]glucose and [(3)H]glucose is attained within 2-3min after injection. 6. The apparent replacement rates for lactate were calculated from the areas under the specific-radioactivity curves or plateau specific radioactivities after primed infusion. Results calculated from bolus injection and infusion agreed closely. The apparent replacement rate for [(3)H]lactate from the A-VC mode averaged about 16mg/min per kg body wt. and that in the V-A mode about 8.5mg/min per kg body wt. The apparent rates for [(14)C]lactate (;rate of irreversible disposal') were 8mg/min per kg body wt. for the A-VC mode and 5.5mg/min per kg body wt. for the V-A mode. Apparent recycling of lactate carbon was 55-60% according to the A-VC mode and 35% according to the V-A mode. 7. The specific radioactivities of [U-(14)C]glucose at isotopic steady state were 55% and 45% that of [U-(14)C]lactate in the A-VC and V-A modes respectively. We calculated, correcting for the dilution of (14)C in gluconeogenesis via oxaloacetate, that over 70% of newly synthesized glucose was derived from circulating lactate. 8. Recycling of (3)H between lactate and glucose was evaluated. It has no significant effect on the calculation of the replacement rate, but affects considerably the areas under the wash-out curves for both [2-(3)H]- and [3-(3)H]-lactate, and calculation of mean transit time and total lactate mass in the body. Corrected for recycling, in the A-VC mode the mean transit time is about 3min, the lactate mass about 50mg/kg body wt. and the lactate space about 65% of body space. The V-A mode yields a mass and lactate space about half those with the A-VC mode. 9. The area under the wash-out curve for [(14)C]lactate is some 20-30 times that for [(3)H]lactate, and apparent carbon mass is 400-500mg/kg body wt. and presumably includes the carbon of glucose, pyruvate and amino acids, which are exchanging rapidly with that of lactate.
| S-EPMC1162777 | biostudies-other