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1.
Asian Pacific Journal of Tropical Biomedicine ; (12): 275-278, 2011.
Article in Chinese | WPRIM | ID: wpr-500345

ABSTRACT

Objective: To analyze the amino acid sequence composition, secondary structure, the spatial conformation of its domain and other characteristics of Argonaute protein. Methods:Bioinformatics tools and the internet server were used. Firstly, the amino acid sequence composition features of the Argonaute protein were analyzed, and the phylogenetic tree was constructed. Secondly, Argonaute protein’s distribution of secondary structure and its physicochemical properties were predicted. Lastly, the protein functional expression form of the domain group was established through the Phyre-based analysis on the spatial conformation of Argonaute protein domains. Results: 593 amino acids were encoded by Argonaute protein, the phylogenetic tree was constructed, and Argonaute protein’s distribution of secondary structure and its physicochemical properties were obtained through analysis. In addition, the functional expression form which comprised the N-terminal PAZ domain and C-terminal Piwi domain for the Argonaute protein was obtained with Phyre. Conclusions: The information relationship between the structure and function of the Argonaute protein can be initially established with bioinformatics tools and the internet server, and this provides the theoretical basis for further clarifying the function of Schistosoma Argonaute protein.

2.
Asian Pacific Journal of Tropical Biomedicine ; (12): 275-278, 2011.
Article in English | WPRIM | ID: wpr-335030

ABSTRACT

<p><b>OBJECTIVE</b>To analyze the amino acid sequence composition, secondary structure, the spatial conformation of its domain and other characteristics of Argonaute protein.</p><p><b>METHODS</b>Bioinformatics tools and the internet server were used. Firstly, the amino acid sequence composition features of the Argonaute protein were analyzed, and the phylogenetic tree was constructed. Secondly, Argonaute protein's distribution of secondary structure and its physicochemical properties were predicted. Lastly, the protein functional expression form of the domain group was established through the Phyre-based analysis on the spatial conformation of Argonaute protein domains.</p><p><b>RESULTS</b>593 amino acids were encoded by Argonaute protein, the phylogenetic tree was constructed, and Argonaute protein's distribution of secondary structure and its physicochemical properties were obtained through analysis. In addition, the functional expression form which comprised the N-terminal PAZ domain and C-terminal Piwi domain for the Argonaute protein was obtained with Phyre.</p><p><b>CONCLUSIONS</b>The information relationship between the structure and function of the Argonaute protein can be initially established with bioinformatics tools and the internet server, and this provides the theoretical basis for further clarifying the function of Schistosoma Argonaute protein.</p>


Subject(s)
Animals , Argonaute Proteins , Chemistry , Genetics , Chemical Phenomena , Cluster Analysis , Computational Biology , Methods , Models, Molecular , Phylogeny , Protein Conformation , Schistosoma , Chemistry , Genetics , Sequence Homology, Amino Acid
3.
Basic & Clinical Medicine ; (12)2006.
Article in Chinese | WPRIM | ID: wpr-594432

ABSTRACT

Objective To prepare polyclonal antibodies against human PIWIL and to identify their property and tissue distribution of PIWIL.Methods PIWIL polypeptide was synthesized and conjugated to Keyhole limpet hemocyanin(KLH) as an immunogen.Then PIWIL-KLH conjugations were injected into rabbits subcutaneously to produce polyclonal antibodies.The specificity and sensitivity of antibodies were identified by ELISA and Western blot after purification by affinity chromatography.PIWIL were then stained on the tissue chip to study their distribution.Results Rabbit antibodies against PIWIL were prepared after injection of PIWIL-KLH conjugation.These antibodies specially recognized PIWIL peptides.Expression of PIWIL was found in the cytoplasm of epithelia cells of varied normal tissues and tumor tissues.Conclusion The successful preparation of the polyclonal antibody against PIWIL will provide an efficient reagent for further study of its role in the pathway of miRNA and RNA interference and in the pathogenesis of human disease.

4.
Journal of Medical Postgraduates ; (12)2003.
Article in Chinese | WPRIM | ID: wpr-591942

ABSTRACT

The PIWI family members are defined as conserved PAZ and PIWI domains and play important roles in stem-cell self-renewal,spermatogenesis,RNA interference and translational regulation.Recent researches have showen that some PIWI are specifically expressed in tumors and associated with tumor development and growth.PIWI is likely to be a new significante index for tumor diagnose and prognosis,the feasibility of PIWI acting in tumor gene theropy could be in vestigated by studying the mechanism of PIWI expression and regulation.

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