Library

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
  • 1
    Electronic Resource
    Electronic Resource
    EMBRYONIC GLOBINS OF THE MARSUPIAL THE TAMMAR WALLABY (MACROPUS EUGENII): BIRD LIKE AND MAMMAL LIKE (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 25 (1998), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Tammar Wallaby embryonic blood has been shown to have three α-like and two β-like globin chains in its four haemoglobin components and partial sequences of several chains have been determined.2. The major embryonic β-like chain (ɛ) is similar to other mammalian embryonic p-like chains on the basis of sequencing its first 60 amino acids.3. There is another embryonic β-like chain present in one haemoglobin component. It was designated to and, in its first 54 amino acids, it has features that are more like avian globins than mammalian globins.4. The one α-like embryonic globin sequenced has mammalian rather than avian characteristics.5. A provisional phylogenetic tree of β-like globins has been determined. The Tammar ω-globin forms a monophyletic group with marsupial and other mammalian embryonic globins; the to-globin forms a monophyletic group with bird adult and embryonic globins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1998.tb02288.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Characterization of Human Plasma Glycoproteins Separated by Two-Dimensional Gel Electrophoresis (1996)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 14 (1996), S. 66-70 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Purification of protein isoforms for the characterization of post-translational modifications, such as glycosylation, can be laborious and demanding. We report a means of determining monosaccharide composition and the identity of glycoproteins from a single spot on a two-dimensional (2-D) gel. The ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0196-66
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    From Proteins to Proteomes: Large Scale Protein Identification by Two-Dimensional Electrophoresis and Arnino Acid Analysis (1996)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 14 (1996), S. 61-65 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Separation and identification of proteins by two-dimensional (2-D) electrophoresis can be used for protein-based gene expression analysis. In this report single protein spots, from polyvinylidene difluoride blots of micropreparative E. coli 2-D gels, were rapidly and economically identified by ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0196-61
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    How to find, identify and quantitate the sugars on proteins (1997)
    [s.l.] : Nature Publishing Group
    Nature 385 (1997), S. 557-559 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The 'one gene-one polypeptide' paradigm is looking outdated as we now understand that in eukaryotes, and even prokaryotes, the output of many genes is post-translationally modified, creating multiple gene products1. While there are a plethora of co- and post-translational modifications, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/385557a0
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Characterization of a major sporozoite surface glycoprotein of Cryptosporidum parvum (2000)
    Springer
    Functional & integrative genomics 1 (2000), S. 207-217 
    Details
    ISSN: 1438-7948
    Keywords: Cryptosporidium parvum Sporozoites Surface glycoprotein S60
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. We have identified S60, a new Cryptosporidium parvum sporozoite surface glycoprotein. S60 was cleaved into two subunits, S16 and S45, approximately 16–18 and 45–47 kDa respectively, with cleavage occurring at an SRSRR motif likely to be sensitive to trypsin in vivo. Analysis by surface biotinylation, lectins and monoclonal antibodies suggests S60 is an abundant sporozoite surface glycoprotein that is shed by migrating sporozoites. The major glycosylation on S60 was identified as single O-linked N-acetylgalactosamine sugars on threonine and serine residues. The gene encoding the S60 protein was identified and revealed a C-terminal consensus sequence for the addition of a glycosylphosphatidyl inositol anchor. Antisera raised against recombinant S60 produced in Escherichia coli reacted with the surface of sporozoites and the inner wall of excysted oocysts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s101420000028
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    NetOglyc: Prediction of mucin type O-glycosylation sites based on sequence context and surface accessibility (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 115-130 
    Details
    ISSN: 1573-4986
    Keywords: mucin type O-glycosylation ; specificity ; GalNAc transferase ; prediction ; neural networks ; gp120 ; SIV ; HIV
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The specificities of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases which link the carbohydrate GalNAc to the side-chain of certain serine and threonine residues in mucin type glycoproteins, are presently unknown. The specificity seems to be modulated by sequence context, secondary structure and surface accessibility. The sequence context of glycosylated threonines was found to differ from that of serine, and the sites were found to cluster. Non-clustered sites had a sequence context different from that of clustered sites. Charged residues were disfavoured at position – 1 and +3. A jury of artificial neural networks was trained to recognize the sequence context and surface accessibility of 299 known and verified mucin type O-glycosylation sites extracted from O-GLYCBASE. The cross-validated NetOglyc network system correctly found 83% of the glycosylated and 90% of the non-glycosylated serine and threonine residues in independent test sets, thus proving more accurate than matrix statistics and vector projection methods. Predictions of O-glycosylation sites in the envelope glycoprotein gp120 from the primate lentiviruses HIV-1, HIV-2 and SIV are presented. The most conserved O-glycosylation signals in these evolutionary-related glycoproteins were found in their first hypervariable loop, V1. However, the strain variation for HIV-1 gp120 was significant. A computer server, available through WWW or E-mail, has been developed for prediction of mucin type O-glycosylation sites in proteins based on the amino acid sequence. The server addresses are http://www.cbs.dtu.dk/services/NetOGlyc/ and netOglyc@cbs.dtu.dk.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006960004440
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation (1994)
    Springer
    Glycoconjugate journal 11 (1994), S. 180-186 
    Details
    ISSN: 1573-4986
    Keywords: N-terminal sequencing ; glycoprotein ; glycan analysis ; covalent immobilization ; mass spectrometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered. In the case of heavily glycosylated domains such as theO-glycosylated mucins, which have no available protease sites, this approach is not possible. Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid. Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection. The PTH-Asn(Sac) derivative was further characterized by ionspray mass spectrometry. Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731216
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Towards an automated approach for protein identification in proteome projects (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1941-1949 
    Details
    ISSN: 0173-0835
    Keywords: Proteome ; Automation ; Two-dimensional polyacrylamide gel electrophoresis ; Mass spectrometry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The development of automated, high throughput technologies for the rapid identification of proteins is essential for large-scale proteome projects. While a degree of automation already exists in some stages of the protein identification process, such as automated acquisition of matrix assisted laser desorption ionisation  -  time of flight (MALDI-TOF) mass spectra, efficient interfaces between different stages are still lacking. We report the development of a highly automated, integrated system for large scale identification of proteins separated by two-dimensional gel electrophoresis (2-DE), based on peptide mass fingerprinting. A prototype robotic system was used to image and excise 288 protein spots from an amido black stained polyvinylidene difluoride (PVDF) blot. Protein samples were enzymatically digested with a commercial automated liquid handling system. MALDI-TOF mass spectrometry was used to acquire mass spectra automatically, and the data analysed with novel automated peptide mass fingerprinting database interrogation software. Using this highly automated system, we were able to identify 95 proteins on the basis of peptide mass fingerprinting, isoelectric point and molecular weight, in a period of less than ten working days. Advantages, problems, and future developments in robotic excision systems, liquid handling, and automated database interrogation software are discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191112
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    '98 Escherichia coli SWISS-2DPAGE database update (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1960-1971 
    Details
    ISSN: 0173-0835
    Keywords: Two-dimensional polyacrylamide gel electrophoresis ; Escherichia coli ; SWISS-2DPAGE database ; Immobilized pH gradient ; Sequence tag ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The combination of two-dimensional polyacrylamide gel electrophoresis (2-DPAGE), computer image analysis and several protein identification techniques allowed the Escherichia coli SWISS-2DPAGE database to be established. This is part of the ExPASy molecular biology server accessible through the WWW at the URL address http://www.expasy.ch/ch2d/ch2d-top.html. Here we report recent progress in the development of the E. coli SWISS-2DPAGE database. Proteins were separated with immobilized pH gradients in the first dimension and sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the second dimension. To increase the resolution of the separation and thus the number of identified proteins, a variety of wide and narrow range immobilized pH gradients were used in the first dimension. Micropreparative gels were electroblotted onto polyvinylidene difluoride membranes and spots were visualized by amido black staining. Protein identification techniques such as amino acid composition analysis, gel comparison and microsequencing were used, as well as a recently described Edman “sequence tag” approach. Some of the above identification techniques were coupled with database searching tools. Currently 231 polypeptides are identified on the E. coli SWISS-2DPAGE map: 64 have been identified by N-terminal microsequencing, 39 by amino acid composition, and 82 by sequence tag. Of 153 proteins putatively identified by gel comparison, 65 have been confirmed. Many proteins have been identified using more than one technique. Faster progress in the E. coli proteome project will now be possible with advances in biochemical methodology and with the completion of the entire E. coli genome.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191114
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Identification and purification of the cell surface glycoprotein homologous to PsA in different species of cellular slime mold on the basis of a shared carbohydrate epitope (1990)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 11 (1990), S. 484-491 
    Details
    ISSN: 0192-253X
    Keywords: Dictyostelium ; glycosylation ; cell adhesion ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The monoclonal antibodies MUD1 and MUD50 recognize peptide and carbohydrate epitopes, respectively, on the Dictyoste-lium discoideum developmentally regulated cell surface glycoprotein PsA. PsA is a putative pre-spore cell adhesion molecule during the slug stage and is anchored to the cell membrane via a phos-phatidylinositol glycan. Here we report on the presence of a PsA-like homolog in several Dictyo-stelium species. The MUD1 epitope is mostly confined to the D. discoideum complex, and only one non-D. discoideum strain reacted strongly with this antibody. By contrast, the mAb MUD50 recognises a homologous molecule in several Dictyostelium species that do not react with MUD1. With mAb MUD50 immunoaffinity chromatography, it was possible to purify and obtain an amino-terminal sequence for the PsA homolog from the Dictvoste-lium sp. strain ZA3A and from one strain of D. pur-pureum.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020110525
    Library Location Call Number Volume/Issue/Year 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...