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  • 1
    Electronic Resource
    Electronic Resource
    Countercurrent Heating and Cooling of Granular Solids with Gases (1953)
    s.l. : American Chemical Society
    Industrial & engineering chemistry 45 (1953), S. 1233-1236 
    Details
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ie50522a028
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  • 2
    Electronic Resource
    Electronic Resource
    Peptide transport by germinating barley embryos: Evidence for a single common carrier for di- and oligopeptides (1978)
    Springer
    Planta 138 (1978), S. 217-221 
    Details
    ISSN: 1432-2048
    Keywords: Germination (embryo) ; Hordeum ; Peptides ; Protein ; Storage protein ; Scutellum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Competition for uptake of a range of amino acids and peptides by germinating barley (Hordeum vulgare L.) embryos was studied. Peptides and amino acids show no competition and are apparently absorbed by independent transport systems. However, peptides of widely different structures do compete and it seems that only a single peptide transport system is present in barley embryos, capable of handling both di- and oligopeptides. The ability of physiological peptides to totally inhibit the uptake of glycylsarcosine indicates they share a common uptake system which previously has been shown to have the properties of an active transport process. The characteristics of the barley peptide transport system are compared with those found in other organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00386814
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  • 3
    Electronic Resource
    Electronic Resource
    Analysis of the peptide carrier in the scutellum of barley embryos by photoaffinity labelling (1991)
    Springer
    Planta 186 (1991), S. 44-51 
    Details
    ISSN: 1432-2048
    Keywords: Embryo (peptide carrier) ; Hordeum (embryo, peptide transport) ; Peptide transport ; Photoaffinity probe
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The preparation of a phenylalanine analogue containing an azido group and its incorporation into dipeptides is described. Peptides modified in this way are taken up into barley (Hordeum vulgare L.) scutella via the previously characterized peptide-transport system. Photoactivation of modified peptides in the presence of isolated scutella resulted in irreversible inhibition of peptide uptake in a concentration-dependent manner. Transport of other solutes which share a common mechanism of energy coupling, but which are transported via distinct carriers, was not inhibited after photo-derivatization of scutella with the modified peptides. Derivatization of isolated scutellar tissue with a 14C-labelled peptide analogue, resulted in incorporation of label into two proteins of Mr = 54000 and 41000. Scutellar tissue from early-germinating seeds, which do not show active peptide uptake, did not incorporate label into these polypeptides. It is concluded that these proteins are components of the barley peptide-transport system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201496
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  • 4
    Electronic Resource
    Electronic Resource
    Stereospecificity of peptide transport by germinating barley embryos (1978)
    Springer
    Planta 142 (1978), S. 299-305 
    Details
    ISSN: 1432-2048
    Keywords: Germination ; Hordeum ; Peptide absorption ; Peptide transport ; Stereospecificity ; Storage protein mobilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The stereospecific requirements for peptide transport in the scutellum of germinating barley (Hordeum vulgare) embryos are described. Replacement of an L-amino acid residue in a peptide by its D-stereoisomer decreases the affinity of the peptide for the transport site, leading to a reduction in transport. Substitution of a second D-residue reduces affinity still further. The extent to which transport is inhibited depends upon the position of the D-residue in the primary sequence, with D-residues at the C-terminus of the peptide having the greatest effect. Competition between D- and L-peptides indicates that they both enter via the same transport system. Although D-amino acids can be accumulated when presented as a peptide, these same D-residues are not transported when supplied as the free amino acids. L-Leu-D-leu is accumulated intact against a concentration gradient, indicating the operation of an active transport mechanism that can function without the involvement of peptidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00385081
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  • 5
    Electronic Resource
    Electronic Resource
    Peptide transport by germinating barley embryos: Uptake of physiological di- and oligopeptides (1978)
    Springer
    Planta 138 (1978), S. 211-215 
    Details
    ISSN: 1432-2048
    Keywords: Germination (embryos) ; Hordeum ; Oligopeptides ; Peptide absorption and transport ; Storage protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The uptake of a variety of physiological di- and oligopeptides by germinating barley (Hordeum vulgare L.) embryos is described. Peptides as large as pentaalanine can be absorbed. Evidence is presented suggesting the peptides are absorbed intact and subsequently undergo rapid intracellular hydrolysis. Uptake shows stereospecificity. The transport of peptides is generally faster than the transport of amino acids, making it likely that the former could play an important role in the mobilization of the protein storage reserves during germination. The peptide transport system in barley is compared with similar systems from other groups of organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00386813
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  • 6
    Electronic Resource
    Electronic Resource
    Peptide transport by germinating barley embryos (1977)
    Springer
    Planta 134 (1977), S. 205-206 
    Details
    ISSN: 1432-2048
    Keywords: Germination ; Hordeum ; Peptide absorption ; Peptide transport ; Scutellum ; Storage proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glycylsarcosine, a dipeptide which is resistant to peptidase activity, was accumulated intact against a concentration gradient by germinating embryos of Hordeum vulgare L., var. Maris Otter, Winter. This is the first clear evidence for the presence of a dipeptide transport system involved in the movement of protein reserves across the scutellum from the endosperm to the embryo during germination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384973
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of active dipeptide transport by germinating barley embryos: Effects of pH and metabolic inhibitors (1977)
    Springer
    Planta 136 (1977), S. 71-76 
    Details
    ISSN: 1432-2048
    Keywords: Germination ; Hordeum ; Peptide absorption ; Peptide transport ; Protein mobilization ; Storage protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A sensitive new fluorescent method is outlined for the study of peptide and amino acid transport processes. Studies on dipeptide transport in germinating barley (Hordeum vulgare.) embryos have provided evidence for accumulation of substrate against a concentration gradient, saturation kinetics, a pH optimum at pH 3.8, and inhibition by a variety of metabolic inhibitors. Acetate also inhibits transport, possibly by disrupting H+ gradients across the plasma membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00387928
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis of the peptide-transport carrier of barley scutellum during the early stages of germination (1985)
    Springer
    Planta 164 (1985), S. 550-556 
    Details
    ISSN: 1432-2048
    Keywords: Germination (seed) ; Hordeum (peptide transport) ; Peptide transport ; Protein synthesis ; Scutellum ; Seed germination ; Thiol group
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Development of peptide-transport activity in the scutella of isolated barley (Hordeum vulgare l. cv. Maris Otter, Winter) embryos is shown to increase rapidly after about 15 h of imbibition, with the bulk of the transport activity being expressed by 24 h. This development is prevented by treatment of 15 h embryos with cycloheximide. Protein synthesis is found to increase in a closely related manner and also to be abolished by cycloheximide. Measurement of the incorporation of bound [35S]methionine by 15 to 21-h embryos indicates that de-novo protein synthesis during this period is greater in the scutellum than in the embryonic axis. Previous studies have shown that the peptide-transport system possesses essential dithiol groups, probably located at the substrate-binding site (Walker-Smith and Payne 1983 b, 1984b). Treatment of 15-h embryos with the non-penetrant thiol reagent p-chloromercuribenzene sulphonic acid did not affect development of peptide-transport activity during the following 6 h, whereas with 3-d embryos identical treatment inhibited uptake almost completely during a subsequent 6-h period. Radioautography revealed that amongst the proteins synthesised during this early phase of germination and labelled in vitro with [35S]methionine some are found within the epithelial plasmalemmae of the scutellum, which is the location of the peptide-transport carrier identified previously by externally labelling with a radioactive thiol reagent. The results provide evidence that protein(s) of the peptide-transport system are synthesised and inserted into the scutellum during early germination, allowing the system to play a major role in the nitrogen nutrition of the embryo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00395974
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  • 9
    Electronic Resource
    Electronic Resource
    Characteristics of the active transport of peptides and amino acids by germinating barley embryos (1984)
    Springer
    Planta 162 (1984), S. 159-165 
    Details
    ISSN: 1432-2048
    Keywords: Amino acid transport ; Germination (seed) ; Hordeum (peptide) ; Peptide transport ; Scutellum ; Storage protein mobilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Use of two different assays involving either radioactively labelled substrates or a fluorescent-labelling procedure, gave good agreement for the rates of transport of peptides and amino acids into the scutellum of germinating grains of barley (Hordeum vulgare cv. Maris Otter, Winter). However, evidence was obtained for the enzymic decarboxylation of transpored substrate, which can cause underestimates of transport rates when using radioactively labelled substrates. The peptide Gly-Phe, was shown to be rapidly hydrolysed after uptake, and autoradiography of transported Gly-[U-14C]Phe indicated a rapid distribution of tracer, i.e. [U-14C] phenylalanine into the epithelium and sub-epithelial layers of the scutellum. The developmental patterns of transport activity indicate that peptide transport is more important nutritionally during the early stages of germination (1–3 d) whereas amino acids become relatively more important later (4–6 d). A range of amino acids is shown to be actively transported and several compete for uptake. At physiological concentrations, e.g. 2mM, transport of peptides and amino acids is inhibited about 80% by protonophore uncouplers, but at higher concentrations (10–100 mM) passive uptake predominates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410213
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  • 10
    Electronic Resource
    Electronic Resource
    Characteristics of the protein carrier of the peptide-transport system in the scutellum of germinating barley embryos (1984)
    Springer
    Planta 162 (1984), S. 166-173 
    Details
    ISSN: 1432-2048
    Keywords: N-Ethylmalemide ; Germination (seed) ; Hordeum (embryo, peptide) ; Peptide transport ; Thiol group ; Transport carrier protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Through the use of the protein reagents N-ethylmaleimide, p-chloromercuribenzenesulphonic acid and phenylarsine oxide, it is shown that in the scutellum of the germinating barley embryo, the transport of peptides, but not the transport of amino acids or glucose is specifically thiol-dependent. Furthermore, these essential thiol groups are shown to exist as redox-sensitive, vicinal-dithiols that lie at the substrate-binding sites of the peptide-transport proteins. The binding of N-ethylmaleimide to these dithiols is shown to be very fast, matching the kinetics of inhibition of peptide transport by this reagent. A technique for the specific labelling of the dithiols with N-ethyl[2,3-14C]maleimide is described, which allows the carrier proteins to be visualized at the scutellar epithelium using radioautography and permits calculation of the approximate amount of peptide-transport protein present per scutellum. In related studies, the importance of arginyl and histidyl residues to both amino-acid and peptide transport is shown, although other residues, e.g. carboxyl ligands do not seem to be critically involved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410214
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