نتایج جستجو برای: gp55

تعداد نتایج: 101  

Journal: :The Journal of biological chemistry 1982
E Polonoff C A Machida D Kabat

Addition of asparagine-linked oligosaccharides to nascent murine leukemia virus (MuLV)-encoded membrane glycoproteins was inhibited either completely by tunicamycin or specifically at Asn-X-Thr glycosylation sites by incorporation of the threonine analogue beta-hydroxynorvaline. In conditions of partial analogue substitution, a series of subglycosylated components is formed which are related by...

Journal: :Cancer research 1976
R E Zachrau M M Black A S Dion B Shore M Isac A M Andrade C J Williams

Cryostat sections of clinicopathologically characterized breast cancer tissues were eluted with phosphate-buffered 0.9% sodium chloride solution, pH 7.2. The proteins were then characterized by polyacrylamide gel electrophoresis with and without prior treatment with sodium dodecyl sulfate. Approximately 65% of the brease cancer tissue eluates contained a prominent protein fraction with a molec...

Journal: :Journal of clinical microbiology 1985
J K Collins A C Butcher C A Riegel

The virus specificity of antibodies against bovine herpes virus type 1 was determined with a radioimmunoprecipitation assay and serum collected from natural and experimentally induced infections. By using sequentially collected sera, the development of antibodies to 4 to 5 viral glycoproteins and 11 to 12 nonglycosylated proteins was followed for the first 50 days after infection. The major and...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2000
K H Smalla H Matthies K Langnäse S Shabir T M Böckers U Wyneken S Staak M Krug P W Beesley E D Gundelfinger

Neuroplastin-65 and -55 (previously known as gp65 and gp55) are glycoproteins of the Ig superfamily that are enriched in rat forebrain synaptic membrane preparations. Whereas the two-Ig domain isoform neuroplastin-55 is expressed in many tissues, the three-Ig domain isoform neuroplastin-65 is brain-specific and enriched in postsynaptic density (PSD) protein preparations. Here, we have assessed ...

Journal: :Infection and immunity 1998
B Banerjee P A Greenberger J N Fink V P Kurup

The 37-kDa recombinant protein Asp f 2, encoding an allergen of Aspergillus fumigatus, was expressed in a prokaryotic expression system and immunologically evaluated for its functional and structural properties. The open reading frame for a 310-amino-acid-long protein was shown to encode a signal peptide of 31 amino acids. A native 37-kDa culture filtrate protein and a 55-kDa mycelial glycoprot...

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