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[34] Antibody probes of ribosomal RNA

Glitz, Dohn G. ; Cann, Pauline A. ; Lasater, Linda S. ; Olson, Helen McKuskie

Methods in Enzymology, 1988, Vol.164, p.493-503 [Periódico revisado por pares]

United States: Elsevier Science & Technology

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Título:
[34] Antibody probes of ribosomal RNA
Autor: Glitz, Dohn G. ; Cann, Pauline A. ; Lasater, Linda S. ; Olson, Helen McKuskie
Assuntos: Animals ; Antibodies - isolation & purification ; Antibody Formation ; Antigen-Antibody Complex ; Chromatography, High Pressure Liquid - methods ; Immunodiffusion ; Male ; Oligonucleotide Probes - chemical synthesis ; Oligonucleotide Probes - isolation & purification ; Rabbits - immunology ; Ribosomes - ultrastructure ; RNA, Ribosomal - analysis ; RNA, Ribosomal - immunology
É parte de: Methods in Enzymology, 1988, Vol.164, p.493-503
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: This chapter focuses on the RNA structure in the ribosome with an emphasis on immunoelectron microscopy. The chapter has used antibody probes to naturally occurring modified nucleotides, to reagents used in the site-specific modification of ribosomal RNA, and to chemically synthesize modified oligo deoxynucleotide that complement and bind specific ribosomal RNA sequences. The chapter discusses the detail methods for the production and characterization of these antibodies and for their use in the study of ribosome structure. There are significant difficulties in probing the structure of the RNA within the ribosome; the secondary structure of the RNA is extensive, and a considerable portion of each sequence is likely to be buried within the subunits and unavailable to probes. A limited number of natural targets—modified nucleotides or chemically unique sites—occur in each subunit, but most of the RNA is lacking in distinct markers.
Editor: United States: Elsevier Science & Technology
Idioma: Inglês

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[34] Antibody probes of ribosomal RNA

Glitz, Dohn G. ; Cann, Pauline A. ; Lasater, Linda S. ; Olson, Helen McKuskie

United States: Elsevier Science & Technology

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