ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles  (5)
  • Capillary electrophoresis  (3)
  • Endoplasmic reticulum  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Distribution of golgi apparatus-associated polyribosomes across the polarity axis of dictyosomes of wild carrot (Daucus carota L.) (1984)
    Springer
    Protoplasma 123 (1984), S. 221-225 
    Details
    ISSN: 1615-6102
    Keywords: Golgi apparatus ; Endoplasmic reticulum ; Polyribosomes ; Golgi apparatus-associated polyribosomes ; Wild carrot (Daucus carota)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Endoplasmic reticulum-polyribosome-Golgi apparatus associations were a general feature of cells of suspension cultures of wild carrot (Daucus carota L.). Free polyribosomes occurred within the Golgi apparatus zone for all dictyosomes and with equal frequency at all levels within the stack including the most mature or trans face. When evaluated and quantified from electron micrographs, approximately 60% of the dictyosome profiles were characterized by a system of transition elements consisting of part smooth-part rough endoplasmic reticulum. These were encountered most frequently in the immediate vicinity of the immature, forming or cis face, usually toward the periphery of the stacked cisternae. Analysis of serial sections showed that those dictyosome profiles not exhibiting this characteristic did so primarily because of an unfavorable plane of sectioning. All dictyosomes examined in 5 or more serial sections revealed some type of close association with endoplasmic reticulum. Some of the associations were so close that direct connections between Golgi apparatus and endoplasmic reticulum tubules could not be excluded. Also present, especially at the forming or cis face, were small 600 nm transition vesicles with nap-like surface coats on nearly 90% of the dictyosomes examined. More than 50% exhibited spiny (clathrin-)coated vesicles at the mature or trans face.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01281169
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Fractionation of suspension cultures of wild carrot and kinetics of membrane labeling (1984)
    Springer
    Protoplasma 123 (1984), S. 213-220 
    Details
    ISSN: 1615-6102
    Keywords: Carrot suspension cultures ; Dictyosomes ; Endoplasmic reticulum ; Golgi apparatus ; Membrane biogenesis ; Plasma membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Wild carrot (Daucus carota L.) cells, grown in suspension culture, were labeled with radioactive precursors and fractionated into constituent membranes to be analyzed for specific radioactivity. Results show rapid incorporation of [3H] leucine into endoplasmic reticulum (ER)-, Golgi apparatus-, and plasma membrane/tonoplast-enriched fractions. The time lag between incorporation into ER and its appearance in Golgi apparatus or plasma membrane/tonoplast were less than 5 minutes. With an average time of 3–4 minutes for cisternal formation estimated from studies with monensin, and an average of 5 cisternae per dictyosome (total transit time of 15–20 minutes), it was not possible to account for early incorporation of radioactivity into plasma membranes by passage of proteins from ER to plasma membrane via the Golgi apparatus. To account for the findings, it would appear that at least some proteins were delivered to the plasma membrane via the first membranes that exited (i.e., mature face vesicles) from the Golgi apparatus post-pulse and that some of these proteins had been translated and inserted into membranes at or near the mature face of the Golgi apparatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01281168
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Use of a Hepta-tyr glycopeptide antibiotic as chiral selector in capillary electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1742-1751 
    Details
    ISSN: 0173-0835
    Keywords: Antibiotics ; Chiral separations ; Enantiomers ; Drugs ; Herbicides ; Capillary electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A new glycopeptide antibiotic, MDL 63,246 (Hepta-tyr), of the teicoplanin family, has been evaluated in capillary electrophoresis for the resolution of chiral compounds of pharmaceutical and environmental interest. Electrophoretic separations were carried out in a polyacrylamide-coated capillary using the partial filling-counter current mode with aqueous-organic buffers in the pH range 4-6. Experimental parameters affecting resolution, such as antibiotic concentration, buffer pH, organic modifier type and capillary temperature, were studied. The Hepta-tyr antibiotic exhibited a high enantiorecognition capability towards the studied compounds at very low concentrations (1-2 mg/mL). The optimum experimental conditions were achieved by using a buffer at pH 5 containing acetonitrile at 25°C.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191036
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Sample matrix effects on glycopeptide stability by high performance capillary electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 751-756 
    Details
    ISSN: 0173-0835
    Keywords: Glycopeptides ; Matrix ; Stability ; Capillary electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: High performance capillary electrophoresis (CE) of glycoprotein digests frequently reveals extensive microheterogeneity associated with specific protein glycosylation sites. The choice of the sample matrix can influence the electrophoretic migration time, peak shape and resolution, as well as the physical stability of the product glycopeptides. Acetic acid is a frequently employed sample matrix for both capillary electrophoresis and electrospray ionization-mass spectrometry (ESI-MS). Acetic acid appears to enhance the spontaneous hydrolysis of sialic acids from the nonreducing termini of glycopeptides in a time- and concentration-dependent manner, even at 5°C, as evidenced by changes in the electrophoretic mobility and ESI-MS spectra of the resulting glycopeptides. The observed parallel electrophoretic mobility changes for specific glycoforms are consistent with the induction of peptide structure with time. Asialoglycopeptide mobilities were stable in acetic acid. Electrophoretic mobilities can be stabilized with propionic acid sample matrix with no apparent structural changes observed by ESI-MS within 31 h. Migration time reproducibility was in the range of 0.1% relative standard deviation (N = 7) with excellent peak shapes and enhanced glycopeptide resolution.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180515
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Peptide capillary zone electrophoresis mass spectrometry of recombinant human erythropoietin: An evaluation of the analytical method (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2654-2664 
    Details
    ISSN: 0173-0835
    Keywords: Glycoprotein ; Glycopeptide ; Peptide ; Capillary electrophoresis ; Mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An evaluation of capillary zone electrophoresis-mass spectrometry (CZE-MS) as an analytical methodology for the separation and characterization of complex glycopeptides and nonglycopeptide structures has been performed. The evaluation employed endoproteinase V8 digested recombinant human erythropoietin (rHuEPO) that was further fractionated by reverse phase chromatography. The peptides were subjected to sequence analysis and evaluated by capillary electrophoresis, with or without mass detection, for peptide purity. The peptide mass determined from the sequence was then compared to the mass obtained from CZE-MS. Glycosylation sites and carbohydrate branch patterns were easily determined, site specific microheterogeneity (either O-acetylation of N-acetylneur-aminic acids or lactosamine extensions of the carbohydrate chain length) was assessed directly, glycosylation site occupancy was evaluated qualitatively, and nonglycopeptides were resolved and analyzed on-line with ease. Incomplete peptide digestion products were detected and identified by CZE-MS. Protein sequence coverage by CZE-MS was 98.2 percent complete from a single map. Offline evaluation of peptide purity by CZE greatly aided the interpretation of multiple sequence analysis and, in validating that, the CZE-MS was detecting all peptides present. All off-line CZE and on-line CZE-MS experiments employed a capillary that was dynamically coated with Polybrene in the presence of polyethylene glycol; separations were conducted in 0.67 M formic acid.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191515
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...