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At least 19 recordsLinked to original sources
PubMed1979

Immunoprecipitation of biosynthetically-labelled products in the identification of antigens of murine red cells infected with the protozoan parasite, Plasmodium berghei.

In this methodological paper an immunoprecipitation technique has been optimised for the identification of antigens of Plasmodium berghei-infected blood which react with antibody specificities in a host-protective antiserum. Extracted 3H-leucine biosynthetically-labelled products of infected blood were sequentially reacted and precipitated with sera from mice which had been exposed to P. berghei but which were either non-protected or protected against lethal infection, protection having been shown to be transferable to naive recipients with the appropriate serum. As analysed by polyacrylamide gel electrophoresis under reducing conditions, a small number of molecular species was detected in immunoprecipitates using host-protective sera which were apparently not quantitatively precipitated out of the complex mixture of labelled products of infected blood using sera from non-protected mice.

Animals↗
PubMed1976

Partial amino-acid sequence of the precursor of an immunoglobulin light chain containing NH2-terminal pyroglutamic acid.

Analyses of amino-acid sequences of the total cell-free products programmed by the mRNA of MOPC-104E gamma light (L)-chain show that over 95% of the products have sequences of a distinct protein that correspond to the L-chain precursor. In this precursor an extra piece is coupled to the NH2-terminus of the mature L-chain. Analyses of products labeled with [3H]alanine, [3H]leucine, and [3H]proline demonstrate that the extra piece is composed of at least 18 residues. Analyses of [35S]methione-labeled product indicate that the extra piece may contain an additional NH2-terminal methionine, which is detected in about 10% of the molecules. Partial recovery of the NJ2-terminal methionine (alanine, leucine, and proline are recovered in yields close to theoretical, greater than 95%) suggests that it is the initiator methionine, which is known to be short lived in eukaryotes due to rapid hydrolysis. Thus, the extra piece seems to be 19 residues in length, and it contains one methionine at the NH2-terminus, three alanines at positions 2, 12, and 17, and five leucines at positions 6, 8, 10, 11, and 13. The close gathering of leucine residues, as well as their abundance (26%), suggest that the extra piece would be quite hydrophobic. Hydrophobicity seems to be a general property of the extra piece, since similar clusters of leucine were found in the precursors of 3 KL-chains (Burstein, Y. & Schechter, I. (1976) Biochem. J. 157, 145-151). The NH2-terminus of the mature MOPC-104E gamma L-chain is blocked by pyroglutamic acid. The fact that in the precursor a peptide segment precedes this NH2-terminus establishes that pyroglutamic acid is not the initiator residue for synthesis of the L-chain. Apparently, the pyroglutamic acid is formed by cyclization of glutamic acid or glutamine during cleavage of the extra piece to yield the mature L-chain.

Amino Acid Sequence↗
PubMed1977

Rat liver preproalbumin: in vitro synthesis and partial amino acid sequence.

Rat liver poly(A)-containing RNA greatly stimulated incorporation of radioactive amino acids into protein when added to a wheat germ in vitro translation system. Approximately 7% of the labeled synthetic product was precipitated following indirect immunoprecipitation with antisera to rat serum albumin. Analysis of this material, and of the cyanogen bromide fragments derived from it, by sodium dodecyl sulfate/polyacrylamide gel electrophoresis revealed that it contained an NH2-terminal extension of about 2500 daltons when compared to rat serum albumin. Automated sequence determination of purified cell-free product labeled with various radioactive amino acids revealed the presence of 18 additional amino acids NH2-terminal to the sequence of rat proalbumin. The partial sequence of this extension was found to be: Met-X-X-X-X-Phe-Leu-Leu-Leu-Leu-Phe-X-X-X-X-X-Phe-X-proalbumin. On the basis of this evidence, the immunoprecipitable cell-free product was designated preproalbumin.

Amino Acid Sequence↗
PubMed1979

Biosynthesis in vitro of immunoreactive 31,000-dalton corticotropin/beta-endorphin-like material by bovine hypothalamus.

Enzymatically dispersed bovine hypothalamic or cortical tissue was maintained in culture in the presence of (3)H-labeled amino acids. After such incubation, extracts of cells and of media contained (3)H-labeled products that were specifically bound by immobilized affinity-purified antisera to corticotropin (ACTH) and beta-endorphin. The majority of these products eluted in the void volume (V(0)) upon Sephadex G-50 gel filtration; minor (3)H-labeled products eluted in the regions of the ovine beta-lipotropin marker and in fractions having apparent molecular weights of approximately 12,000 and 3800. Sequential use of these immobilized antisera revealed that most of the V(0) material contained both ACTH and beta-endorphin antigenic determinants within the same molecule(s), whereas retarded material contained only one of the determinants. When this V(0) material was rerun on a Sephadex G-75 column, it coeluted with the 31-kilodalton precursor of both ACTH and beta-endorphin obtained from a bovine anterior pituitary extract. Thus, the high molecular weight immunoreactive ACTH/beta-endorphin-like (3)H-labeled product(s) derived from the hypothalamic culture is similar to the pituitary-derived precursor in containing the dual antigenic determinants and in its gel filtration characteristics. In contrast, the cortex-derived cell preparation was devoid of (3)H-labeled products specifically reactive with the antisera employed.

Adrenocorticotropic Hormone↗
PubMed1975

Tritiation of endotoxin.

Tritiated endotoxin was synthesized by three different methods: (1) sodium boro[3H]hydride reduction of native endotoxin; (2) sodium boro[3H]hydride reduction of endotoxin that had been oxidized previously with sodium metaperiodate; and (3) exposure of dry endotoxin to 3H2 gas. Sodium borohydride reduces aldehyde groups and sodium metaperiodate oxidizes vicinal glycol groups to aldehydes. Chromatographic analysis of the three tritiated endotoxins, using agarose, revealed that the biological activity associated with each labeled product appeared at the void volume, and in each case the biological activity coincided with a peak in radioactivity. The labeled product of the first method had a specific radioactivity of 0.18 mCi/g and a biological activity equal to that of native endotoxin. The labeled products of the second and third methods had specific activities of 2.1 mCi/g and 60.0 mCi/g, respectively, while their biological activities were one hundred-fold less than native endotoxin, as determined by the Limulus amebocyte lysate assay. These three labeled endotoxins are potentially ueled endotoxin.

Biological Assay↗
PubMed1978

Incorporation of labelled degradation products of radioactive thymine into non DNA material.

When thymine auxotrophs are grown in the presence of methyl labelled [3H] or [14C] thymine which has been stored at 4 degrees C, two classes of material are labelled which are not DNA. One class sediments on neutral sucrose gradients with spontaneously single stranded Okazaki pieces, is unstable in alkali, migrates on alkaline gels as very small material and is digested by ribonucleases and micrococcal nuclease, but not by DNAase I. This class is presumably RNA. The second class sediments more slowly on both neutral and alkaline sucrose gradients than Okazaki pieces, but co-migrates on alkaline gels with DNA whose size is between 700 and 4000 nucleotides. It is not digested by alkali, ribonucleases or deoxyribonucleases. Its identity is unknown. The proportion of the total incorporated counts in these two classes depends on the time of storage of the thymine and is already sufficient to interfere with certain types of experiments when the thymine is only a few weeks old. Thymine is easily purified by paper chromatography and this purified thymine does not label the two non DNA classes of material. It is recommended that radioactive thymine be purified in this way before use.

Carbon Radioisotopes↗
PubMed1977

The characterization of phosphoseryl tRNA from lactating bovine mammary gland.

BD-cellulose and RPC-5 chromatography of tRNA isolated from lactating bovine mammary gland showed the presence of four seryl-tRNA isoacceptors. The species, tRNA IV Ser, with the strongest affinity for BD-cellulose (required ethanol in the elution buffer) could be phosphorylated in the presence of serine, [gamma-32 P]-ATP, seryl-tRNA synthetase and phosphotransferase activity from the same tissue. O-Phosphoserine was identified as the 32P-labelled product after mild alkaline hydrolysis of this aminoacylated tRNA. Pancreatic ribonuclease treatment of the aminoacylated tRNA yielded a labelled product which was identified as phosphoseryladenosine. These results indicated there is a specific phosphoseryl tRNA species in lactating bovine mammary gland. It appears that the formation of phosphoseryl-tRNA proceeds by enzymic phosphorylation of seryl-tRNA.

Amino Acyl-tRNA Synthetases↗
PubMed1978

The mechanism of acceptor reactions of Leuconostoc mesenteroides B-512F dextransucrase.

Reactions of dextransucrase and sucrose in the presence of sugars (acceptors) of low molecular weight have been observed to give a dextran of low molecular weight and a series of oligosaccharides. The acceptor reaction of dextransucrase was examined in the absence and presence of sucrose by using D-[14C]glucose, D-[14C]fructose, and 14C-reducing-end labeled maltose as acceptors. A purified dextransucrase was preincubated with sucrose, and the resulting D-fructose and unreacted sucrose were removed from the enzyme by chromatography of columns of Bio-Gel P-6. The enzyme, which migrated at the void volume was collected and referred to as "charged enzyme". The charged enzyme was incubated with 14C-acceptor in the absence of sucrose. Each of the three acceptors gave two fractions of labeled products, a high molecular weight product, identified as dextran, and a product of low molecular weight that was an oligosaccharide. It was found that all three of the acceptors were incorporated into the products at the reducing end. Similar results were obtained when the reactions were performed in the presence of sucrose, but higher yields of labeled products were obtained and a series of homologous oligosaccharides was produced when D-glucose or maltose was the acceptor. We propose that the acceptor reaction proceeds by nucleophilic displacement of glucosyl and dextranosyl groups from a covalent enzyme-complex by a specific, acceptor hydroxyl group, and that this reaction effects a glycosidic linkage between the D-glucosyl and dextranosyl groups and the acceptor. We conclude that the acceptor reactions serve to terminate polymerization of dextran by displacing the growing dextran chain from the active site of the enzyme; the acceptors, thus, do not initiate dextran polymerization by acting as primers.

Chromatography, Paper↗
PubMed1978

Evidence that triiodothyronine and reverse triiodothyronine are sequentially deiodinated in man.

We have demonstrated that in patients given a single iv injection of T3, rT3, or, to a lesser extent, T4, all labeled with 125I in the outer or phenolic ring, chromatography of serum on columns of Sephadex G-25 superfine revealed the presence of a labeled material, separate from the administered hormone and from both iodide and iodoprotein. This peak has been termed pre-T3 because it elutes just before the T3 peak. Identification of the various compounds in pre-T3 was carried out by cation exchange chromatography. Pre-T3 generated from [125I]T3 consistently contained labeled compounds with the chromatographic behavior of 3,3'-diiodothyronine and 3'-monoiodothyronine, while pre-T3 generated from [125I]rT3 contained labeled products with the chromatographic mobility of 3',5'-diiodothyronine, 3,3'-diiodothyronine, and 3'-monoiodothyronine. In addition, pre-T3 also contained the glucuro- and sulfoconjugates of these several labeled products. These studies demonstrate that T3 and rT3 undergo progressive and probably sequential deiodination in the peripheral tissues, resulting in the formation of a variety of diiodothyronines and monoiodothyronine, as well as their glucuro- and sulfoconjugates.

Animals↗
PubMed1975

Enzymatic synthesis of a blood group H-related glycosphingolipid by an alpha-fucosyltransferase from bovine spleen.

An alpha-fucosyltransferase activity has been detected in a purified membrane preparation isolated from bovine spleen which catalyzes the transfer of L-fucose from GDP-L-[14C]-fucose to a tetraglycosylceramide (Lac-nTet-cer, Galbetal-4GlcNAcbeta1-3Galbeta1-4-Glc-cer) to form the blood group H-related glycosphingolipid. The membrane preparation contained a highly active endogenous nonlipid acceptor, which could be precipitated by 5% trichloroacetic acid or chloroform-methanol-water (6:3:5, v/v/v), whereas there was little endogenous glycosphingolipid acceptor. The optimum pH value for the incorporation of L-fucose was 6.4 in cacodylate-HCl buffer. The Km values were 0.6 mM and 0.36 mM for Lac-nTet-cer and GDP-L-fucose, respectively. The 14C-labeled product of the reaction was isolated and purified; it migrated with human erythrocyte blood group H-active pentaglycosylceramide. the terminal [14C]fucose was hydrolyzed 85% and 55% by 0.1 N trichloroacetic acid at 100 degrees for 2 hours and Charonia lampas alpha-fucosidase (19 hours at 37 degrees), respectively. The 14C-labeled product inhibited the hemagglutination reaction of O-type cells against eel anti H(O) globulin and formed a precipitin line with Ulex europeus lectin.

Animals↗
PubMed1979

Medications not to be refrigerated.

A survey of selected drug labelers was conducted to generate a list of drug products that should not be refrigerated. Letters asking for information on products adversely affected by refrigeration were mailed to 109 drug product labelers. A second letter was sent to nonresponders and to labelers providing incomplete information. Responses were received from 97 labelers, 43 of whom stated that none of their products would be harmed by refrigeration. Eleven labelers were unable to provide conclusive data or a list of specific drug products that refrigeration would harm. Lists of drug products not to be refrigerated were provided by 43 labelers, some including explanations of the adverse effects of refrigeration. Pharmacists may find the survey's data useful in their patient education activities.

Drug Labeling↗
PubMed1976

Legal implications of preparing and dispensing drugs under conditions not in a product's official labeling.

The legal issues surrounding the potential liability of a pharmacist for dispensing or preparing drugs under conditions not contained in the official labeling of a product are examined. Although the specific issue of liability of a pharmacist for preparing a drug in a nonapproved manner or dispensing a drug for a nonapproved use has not been adjudicated, based on evolving legal principles it appears that the pharmacist will be held responsible for the drugs so prepared or dispensed. Preparation of a drug which is adulterated under the federal Food, Drug and Cosmetic Act appears to be negligent, although its precise effect will be dependent upon state law. Liability for dispensing for nonapproved uses may be minimized if the pharmacist, in the exercise of sound professional judgment, concludes that the use is rational, safe and reasonable.

Drug Compounding↗
PubMed1978

[Role of pyruvate kinase in non-specific changes of carbon photosynthetic metabolism, caused by the photophosphorylation inhibition].

The decrease in the level of NADP reduction in chloroplasts under injections of cofactors of pseudocyclic FMN photophosphorylation (vitamin K3 and methylviologen) into pea, tomato and cucumber leaves resulted in the decrease of 14CO2 autotrophic accumulation rate and in the change of distribution of assimilated carbon among the assimilation products. The inhibition of synthesis of labelled sugars and the increase of the content of 3-phosphoglyceric and glyceric acids in the labelled low molecular fraction were observed in all the experiments. Similar changes in the distribution of synthesized in Kalvin cycle labelled products, associated with the inhibition of its reduction unit, were observed under the effect of photophosphorylation uncoupling agents. However, the decrease of ATP/NADP ratio in chloroplasts resulted in the simultaneous increase of fixed 14CO2 incorporation into alanine. The role of pyruvate kinase in "alanine" effect, characteristic of non-specific changes of carbon photosynthetic metabolism, is discussed on the basis of the authors' previous data on the effect of phosphorylation on glycolysis reactions and on the basis of results of ADP introduction into leaf cuts.

Alanine↗