scholarly journals Amino acid sequence variations in Nicotiana CRR4 orthologs determine the species-specific efficiency of RNA editing in plastids

2008 ◽  
Vol 36 (19) ◽  
pp. 6155-6164 ◽  
Author(s):  
Kenji Okuda ◽  
Yuya Habata ◽  
Yoshichika Kobayashi ◽  
Toshiharu Shikanai
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rna Editing ◽  
Sequence Variations ◽  
Species Specific

Lagomorph IgG hinge region: Allotype associated amino acid sequence variations

1976 ◽  
Vol 13 (3) ◽  
pp. 215-220 ◽  
Author(s):  
Shanti J. Aggarwal ◽  
William J. Mandy
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Hinge Region ◽  
Sequence Variations

scholarly journals Analysis of Amino Acid Sequence Variations and Immunoglobulin E-Binding Epitopes of German Cockroach Tropomyosin

2004 ◽  
Vol 11 (5) ◽  
pp. 874-878 ◽  
Author(s):  
Kyoung Yong Jeong ◽  
Jongweon Lee ◽  
In-Yong Lee ◽  
Han-Il Ree ◽  
Chein-Soo Hong ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Single Molecule ◽  
Immunoglobulin E ◽  
German Cockroach ◽  
Amino Acid Sequences ◽  
Enzyme Linked Immunosorbent Assay ◽  
Rt Pcr ◽  
Ige Binding ◽  
Sequence Variations

ABSTRACT The allergenicities of tropomyosins from different organisms have been reported to vary. The cDNA encoding German cockroach tropomyosin (Bla g 7) was isolated, expressed, and characterized previously. In the present study, the amino acid sequence variations in German cockroach tropomyosin were analyzed in order to investigate its influence on allergenicity. We also undertook the identification of immunodominant peptides containing immunoglobulin E (IgE) epitopes which may facilitate the development of diagnostic and immunotherapeutic strategies based on the recombinant proteins. Two-dimensional gel electrophoresis and immunoblot analysis with mouse anti-recombinant German cockroach tropomyosin serum was performed to investigate the isoforms at the protein level. Reverse transcriptase PCR (RT-PCR) was applied to examine the sequence diversity. Eleven different variants of the deduced amino acid sequences were identified by RT-PCR. German cockroach tropomyosin has only minor sequence variations that did not seem to affect its allergenicity significantly. These results support the molecular basis underlying the cross-reactivities of arthropod tropomyosins. Recombinant fragments were also generated by PCR, and IgE-binding epitopes were assessed by enzyme-linked immunosorbent assay. Sera from seven patients revealed heterogeneous IgE-binding responses. This study demonstrates multiple IgE-binding epitope regions in a single molecule, suggesting that full-length tropomyosin should be used for the development of diagnostic and therapeutic reagents.

scholarly journals Purification, Characterization, and Molecular Analysis of the Gene Encoding Glucosyltransferase fromStreptococcus oralis

2000 ◽  
Vol 68 (5) ◽  
pp. 2475-2483 ◽  
Author(s):  
Taku Fujiwara ◽  
Tomonori Hoshino ◽  
Takashi Ooshima ◽  
Shizuo Sobue ◽  
Shigeyuki Hamada
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pcr Primers ◽  
Water Soluble ◽  
Oral Streptococci ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
Streptococcus Sanguis ◽  
Specific Nucleotide Sequence ◽  
Species Specific

ABSTRACT Streptococcus oralis is a member of the oral streptococcal family and an early-colonizing microorganism in the oral cavity of humans. S. oralis is known to produce glucosyltransferase (GTase), which synthesizes glucans from sucrose. The enzyme was purified chromatographically from a culture supernatant of S. oralis ATCC 10557. The purified enzyme, GTase-R, had a molecular mass of 173 kDa and a pI of 6.3. This enzyme mainly synthesized water-soluble glucans with no primer dependency. The addition of GTase markedly enhanced the sucrose-dependent resting cell adhesion of Streptococcus mutans at a level similar to that found in growing cells of S. mutans. The antibody against GTase-R inhibited the glucan-synthesizing activities ofStreptococcus gordonii and Streptococcus sanguis, as well as S. oralis. The N-terminal amino acid sequence of GTase-R exhibited no similarities to known GTase sequences of oral streptococci. Using degenerate PCR primers, an 8.1-kb DNA fragment, carrying the gene (gtfR) coding for GTase-R and its regulator gene (rgg), was cloned and sequenced. Comparison of the deduced amino acid sequence revealed that thergg genes of S. oralis and S. gordonii exhibited a close similarity. The gtfR gene was found to possess a species-specific nucleotide sequence corresponding to the N-terminal 130 amino acid residues. Insertion oferm or aphA into the rgg orgtfR gene resulted in decreased GTase activity by the organism and changed the colony morphology of these transformants. These results indicate that S. oralis GTase may play an important role in the subsequent colonizing of mutans streptoccoci.

Effect of amino acid sequence variations at position 149 on the fusogenic activity of the subtype B avian metapneumovirus fusion protein

2015 ◽  
Vol 160 (10) ◽  
pp. 2445-2453 ◽  
Author(s):  
Bingling Yun ◽  
Yanni Gao ◽  
Yongzhen Liu ◽  
Xiaolu Guan ◽  
Yongqiang Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fusion Protein ◽  
Avian Metapneumovirus ◽  
Fusogenic Activity ◽  
Subtype B ◽  
Sequence Variations

Amino acid sequence variations in protein AA of cats with high and low incidences of AA amyloidosis

1989 ◽  
Vol 94 (4) ◽  
pp. 765-768 ◽  
Author(s):  
K.H. Johnson ◽  
K. Sletten ◽  
R.E. Werdin ◽  
G.T. Westermark ◽  
T.D. O'Brien ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Aa Amyloidosis ◽  
Sequence Variations

Automated Identification of Amino Acid Sequence Variations in Proteins by HPLC/Microspray Tandem Mass Spectrometry

2000 ◽  
Vol 72 (4) ◽  
pp. 757-763 ◽  
Author(s):  
Christine L. Gatlin ◽  
Jimmy K. Eng ◽  
Stacy T. Cross ◽  
James C. Detter ◽  
John R. Yates
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Automated Identification ◽  
Sequence Variations
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