Aminosäuren und Derivate

Brenner, M.; Niederwieser, A.; Pataki, György

doi:10.1007/978-3-642-49187-0_25

Cited by 23 publications

(21 citation statements)

References 153 publications

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“…5554) using the following solvent systems (parts by volume): (1) acet0ne:benzene:methanol:water (8:3:2:1; Yoshida and Uemura, 1986); (2) ch1oroform:acetone:methanol: acetic acid:water (10:4:2:3:1; Yoshida and Uemura, 1986); (3) chloroform:methanol:17% ammonia (2:2: 1; Brenner et al, 1967); (4) phenokwater (3:1, w/v; Brenner et al, 1967); (5) isobutyric acidwater:propanol-1:25% ammonia:propanol-2:butanol-1 (100:19:4:14:3:3; KomoPa et al, 1992). Radioactivity on the TLC plates was monitored by two-dimensional scanning with a TLC linear analyzer (LB 2842, Berthold, Wildbad, Germany).…”

Section: Extracted and Separation Of Metabolite Fractialnsmentioning

confidence: 99%

Detoxification of Formaldehyde by the Spider Plant (Chlorophytum comosum L.) and by Soybean (Glycine max L.) Cell-Suspension Cultures

et al. 1994

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The phytotoxicity of formaldehyde for spider plants (Chlorophytum comosum L.), tobacco plants (Nicotiana tabacum L. cv Bel B and Bel W3), and soybean (Glycine max L.) cell-suspension cultures was found to be low enough to allow metabolic studies. Spider plant shoots were exposed to 7.1 pL L-' (8.5 mg m-3) gaseous ["CIformaldehyde over 24 h. Approximately 88% of the recovered radioactivity was plant associated and was found to be incorporated into organic acids, amino acids, free sugars, and lipids as well as cell-wall components. Similar results were obtained upon feeding ["Clformaldehyde from aqueous solution to aseptic soybean cell-suspension cultures. Serine and phosphatidylcholine were identified as major metabolic products. Spider plant enzyme extracts contained two NAS+-dependent formaldehyde dehydrogenase activities with molecular m a s values of about 129 and 79 kD. Only the latter enzyme activity required glutathione as an obligatory second cofactor. It had an apparent K,,, value of 30 p~ for formaldehyde and an isoelectric point at pH 5.4. Total cell-free dehydrogenase activity corresponded to 13 pg formaldehyde oxidized h-' g-' leaf fresh weight. Clutathione-dependent formaldehyde dehydrogenases were also isolated from shoots and leaves of Equisetum telmateia and from cell-suspension cultures of wheat (Triticum aestivum L.) and maize (Zea mays 1.). The results obtained are consistent with the concept of indoor air decontamination with common room plants such as the spider plant. Formaldehyde appears to be efficiently detoxified by oxidation and subsequent C1 metabolism.

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Section: Extracted and Separation Of Metabolite Fractialnsmentioning

confidence: 99%

Detoxification of Formaldehyde by the Spider Plant (Chlorophytum comosum L.) and by Soybean (Glycine max L.) Cell-Suspension Cultures

et al. 1994

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“…Amino acids were identified as their phenylthiohydantoin derivatives by thinlayer chromatography on silica gel F254 plates (Merck AG., Darmstadt, Germany) using the solvent systems described by Brenner et al [23]. Amino acid sequences of other peptides were determined by the dansylEdman technique as described by Hartley [21].…”

Section: Amino-acid Sequence Determinationsmentioning

confidence: 99%

The Amino-Acid Sequence and Carbohydrate Content of Phospholipase A2 from Bee Venom

et al. 1974

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The complete amino acid sequence of phospholipase A2 from the venom of the common European honey-bee (Apis mellifica) has been determined. The sequence of amino acid residues at the N-terminus was obtained by direct application of the Edman degradation technique and that at the C-terminus by digestion with carboxypeptidasesA and B. Digestion of the reduced and carboxymethylated enzyme with trypsin yielded a completely soluble peptide mixture, all the components of which were isolated and their structures determined. Overlaps of the tryptic peptides were deduced from the structures of peptides isolated after digestion of the reduced and carboxymethylated enzyme with chymotrypsin and of the reduced and aminoethylated enzyme with a protease specific for cleavage at lysine residues. Two remaining ambiguities were resolved by peptides obtained from a digest of the reduced, carboxymethylated and maleylated enzyme with trypsin. The phospholipase A2 consists of a single chain of 128 amino acid residues and contains attached carbohydrate residues. The composition and point of attachment of the carbohydrate moiety have been established. Phospholipase A2 is the name given to a family of enzymes which catalyse the hydrolysis of fatty acid ester bonds at the 2-carbon position of 3-sn-phosphoglycerides. Enzymes with this specificity have been isolated from pancreatic tissue [l], bee venom [2] and a variety of snake venoms [3]. The enzymes have certain characteristics in common, for example relatively small size, high disulphide-bridge content, heat stability and requirement for Ca2+ ions for activity. There are, however, important differences. In particular, the pancreatic enzyme appears to be active on the aggregated (micellar) form of phospholipids [4], whereas the substrate for the bee-venom enzyme has been shown to be the dispersed (monomolecular) phospholipid [2]. It is also of interest that the enzyme from pancreas is secreted as an inactive zymogen which may be activated by limited proteolysis with trypsin sequence of the zymogen and the positions of the disulphide bridges in porcine pancreatic phospholipase A2 have been reported [6,7].Our interest in phospholipase A2 from bee venom arose from the observation [2] that the enzyme crystallises readily which, combined with its relatively small size, suggests that it may be amenable to total structure determination. As a preliminary to crystallographic analysis we have determined the primary structure of the enzyme; this work has been the subject of a preliminary report [S]. A missing overlap in the earlier work has now been established with certainty and three corrections have been made to the previously published sequence. In addition, the composition and point of attachment of the carbohydrate moiety have been established. An interesting aspects of the present work has been the use of a recently characterized protease isolated from the basidiomycete Armillaria mellea [9] ; the enzyme has been shown to have specificity for cleavage of peptide bonds N-terminal to lysin...

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“…Hydrolysis was carried out in sealed ampules during 10 h a t I00 "C. The hydrolysate was lyophilized and analysed chromatographically on silica thinlayer chromatography plates using a phenol -water (75 g : 25 ml) solvent [16]. The position of [32P]phosphoserine was determined by revealing an added unlabeled phosphoserine marker with ninhydrin.…”

Section: The Cell-free System and Product Analysismentioning

confidence: 99%

Isolation and Characterization of Ribosome‐Free Cytoplasmic Messenger‐Ribonucleoprotein Complexes from Avian Erythroblasts

Gander¹,

Stewart²,

Morel³

et al. 1973

European Journal of Biochemistry

104

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Two RNA . protein complexes were isolated from duck erythroblast postribosomal supernatants. Their nominal sedimentation values on sucrose gradients are 12 S and 20 s, respectively. The 12-S particle contains a 4-6 S RNA, in the 20-S particle a 9-S RNA is found. This 9-S RNA is shown to direct the synthesis of all duck globin chains in a cell-free, messenger RNA-dependent protein-synthesizing system.The protein moiety of these ribosome-free particles is described and compared with the proteins found in the mRNA * protein complex liberated by EDTA from polyribosomes. We show that in the free-cytoplasmic particles no protein can be found which is identical to any of the polypeptides associated with polyribosomal mRNA. Some of these proteins are phosphorylated and contain phosphoserine. The electrophoretic patterns of phosphorylated proteins from the two globin mRNA-containing complexes differ, as do those of the unlabelled polypeptides. We conclude that the mRNA-associated protein population is exchanged when the mRNA enters the translation machinery.The possible role of the RNA-associated proteins in the post-transcriptional and translational control of eukaryotic protein synthesis is discussed.On the basis of experiments concerning the nucleic acid metabolism in duck immature red cells and in HeLa cells we postulated [I] that the regulation of gene expression in animal cells resides in a multistep process including the three principal phases of cellular information transfer : (a) the synthesis in the nucleus of giant precursor molecules (pre-mRNA) to messenger RNA (mRNA), (b) the processing of the pre-mRNA which gives rise ultimately to mRNA that is transported (and stored) in the cytoplasm, (c) the translation of the mRNA into protein. This regulational system governing the multiple steps involved in synthesis, processing and translation of mRNA was termed "Cascade Regulation" [l -31. Evidence that the giant nuclear RNA of molecular weight more than 5~1 0~is an informative precursor to mRNA was given recently by Imaizumi et al. [5] who showed conclusively by molecular hybridization that these RNA molecules, isolated from duck erythroblasts, contain sequences homologous to polyribosomal 9-S duck globin mRNA. However, the processing of pre-mRNA and the transfer of mRNA to the cytoplam are still obscure.Abbreviations. pre-mRNA, precursor molecule to mRNA; mRNA * protein, messenger ribonucleoprotein complex. strate that newly synthesized mRNA appears in the cytoplasm first free from ribosomes but associated with proteins in the form of ribonucleoprotein complexes. Some mRNA types then associate with ribosomes; others may be degraded without being translated.

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Aminosäuren und Derivate

Cited by 23 publications

References 153 publications

Detoxification of Formaldehyde by the Spider Plant (Chlorophytum comosum L.) and by Soybean (Glycine max L.) Cell-Suspension Cultures

Detoxification of Formaldehyde by the Spider Plant (Chlorophytum comosum L.) and by Soybean (Glycine max L.) Cell-Suspension Cultures

The Amino-Acid Sequence and Carbohydrate Content of Phospholipase A2 from Bee Venom

Isolation and Characterization of Ribosome‐Free Cytoplasmic Messenger‐Ribonucleoprotein Complexes from Avian Erythroblasts

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