scholarly journals THE RIBOSOMES OF DROSOPHILA. III. RNA AND PROTEIN HOMOLOGY BETWEEN D. MELANOGASTER AND D. VIRILIS

Genetics ◽  
1976 ◽  
Vol 84 (3) ◽  
pp. 573-585
Author(s):  
Lee Weber ◽  
Edward Berger ◽  
Charles Vaslet ◽  
Barry Yedvobnick
Keyword(s):  
Ribosomal Rna ◽  
Sequence Homology ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
Filter Hybridization ◽  
Hemolymph Protein ◽  
Larval Hemolymph ◽  
Species Specific

ABSTRACT The extent of interspecific homology between D. melanogaster and D. virilis for ribosomal RNA and ribosomal protein was examined using the techniques of two-dimensional gel electrophoresis, and RNA-DNA filter hybridization. Only 2 of the 71 ribosomal proteins resolved were found to be species specific, while comparisons of soluble larval hemolymph protein patterns showed little similarity. Depending on the technique employed, the sequence homology for 18S + 28S ribosomal RNA was found to be between 83-94%, and sequence homology for 5S rRNA was judged to be complete.

Analysis of Ribosomal Proteins from a Yellow Mutant of Chlamydomonas reinhardii by Two-dimensional Gel Electrophoresis

1979 ◽  
Vol 174 (9) ◽  
pp. 822-830 ◽  
Author(s):  
István Gyurján ◽  
Géza Erdös ◽  
Nadiezda P. Yurina ◽  
Marina S. Turischeva ◽  
Margarita S. Odintsova
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Chlamydomonas Reinhardii

scholarly journals Binding properties of detergent-solubilized NCAM.

1990 ◽  
Vol 110 (3) ◽  
pp. 817-824 ◽  
Author(s):  
A K Hall ◽  
R Nelson ◽  
U Rutishauser
Keyword(s):  
Gel Electrophoresis ◽  
Binding Proteins ◽  
Polysialic Acid ◽  
Binding Properties ◽  
Two Dimensional Gel Electrophoresis ◽  
Homophilic Binding ◽  
Brain Membrane ◽  
Specific Antibodies ◽  
Frog Brain ◽  
Species Specific

An assay has been designed for the identification of NCAM-binding proteins present in an NP-40 detergent extract of brain membranes. This method, which is capable of analyzing both heterophilic and homophilic interactions, uses species-specific antibodies against NCAM in combination with radioiodination, so that after unlabeled chicken and iodinated frog brain membrane proteins were allowed to interact, the chicken NCAM could be specifically isolated by immunoaffinity adsorption. The radiolabeled frog proteins coisolated with chicken NCAM were then characterized by one- and two-dimensional gel electrophoresis in combination with immunoblotting. The only detectable NCAM-binding proteins were identified as the 140- and 180-kD forms of NCAM. The presence and absence of polysialic acid on NCAM did not change the amount or nature of the frog proteins immunopurified under these conditions. As an alternative for detecting heterophilic ligands, a simplified immunoprecipitation method was employed using either iodine or sulfate radiolabels. Again under these conditions only NCAM was detected. These results are consistent with the hypothesis that the major binding protein for NCAM is NCAM itself, and suggest that differences in polysialic acid content do not directly alter the properties of NCAM's homophilic binding site.

scholarly journals Initial Proteome Analysis of Model Microorganism Haemophilus influenzae Strain Rd KW20

2003 ◽  
Vol 185 (15) ◽  
pp. 4593-4602 ◽  
Author(s):  
Eugene Kolker ◽  
Samuel Purvine ◽  
Michael Y. Galperin ◽  
Serg Stolyar ◽  
David R. Goodlett ◽  
...  
Keyword(s):  
Haemophilus Influenzae ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Protein Identification ◽  
Proteome Analysis ◽  
Tandem Mass ◽  
Two Dimensional ◽  
High Confidence ◽  
Two Dimensional Gel Electrophoresis

ABSTRACT The proteome of Haemophilus influenzae strain Rd KW20 was analyzed by liquid chromatography (LC) coupled with ion trap tandem mass spectrometry (MS/MS). This approach does not require a gel electrophoresis step and provides a rapidly developed snapshot of the proteome. In order to gain insight into the central metabolism of H. influenzae, cells were grown microaerobically and anaerobically in a rich medium and soluble and membrane proteins of strain Rd KW20 were proteolyzed with trypsin and directly examined by LC-MS/MS. Several different experimental and computational approaches were utilized to optimize the proteome coverage and to ensure statistically valid protein identification. Approximately 25% of all predicted proteins (open reading frames) of H. influenzae strain Rd KW20 were identified with high confidence, as their component peptides were unambiguously assigned to tandem mass spectra. Approximately 80% of the predicted ribosomal proteins were identified with high confidence, compared to the 33% of the predicted ribosomal proteins detected by previous two-dimensional gel electrophoresis studies. The results obtained in this study are generally consistent with those obtained from computational genome analysis, two-dimensional gel electrophoresis, and whole-genome transposon mutagenesis studies. At least 15 genes originally annotated as conserved hypothetical were found to encode expressed proteins. Two more proteins, previously annotated as predicted coding regions, were detected with high confidence; these proteins also have close homologs in related bacteria. The direct proteomics approach to studying protein expression in vivo reported here is a powerful method that is applicable to proteome analysis of any (micro)organism.

Sign in / Sign up

Export Citation Format

Share Document