Studies on Ribonuclease T1
نویسندگان
چکیده
منابع مشابه
RNase T1 mimicking artificial ribonuclease
Recently, artificial ribonucleases (aRNases)--conjugates of oligodeoxyribonucleotides and peptide (LR)(4)-G-amide--were designed and assessed in terms of the activity and specificity of RNA cleavage. The conjugates were shown to cleave RNA at Pyr-A and G-X sequences. Variations of oligonucleotide length and sequence, peptide and linker structure led to the development of conjugates exhibiting G...
متن کاملStudies on Ribonuclease S
Specific regions of the polypeptide sequence of pancreatic ribonuclease have been altered by chemical modification and by limited proteolytic digestion in attempts to implicate specific covalent portions of the molecule in the structure and stabilization of the active center. Digestion of the native molecule with trypsin at elevated temperatures has been shown to remove portions of the chain wi...
متن کاملStudies on a nucleoprotein prepared from rat liver polysomes by digestion with T1 ribonuclease.
1. Treatment of rat liver polysomes in a buffer containing 2.5mm-magnesium chloride with T(1) ribonuclease at a concentration of 330units/ml. of reaction medium at 37 degrees for 2hr. leads to the production of an insoluble nucleoprotein. 2. On the bases of analysis for protein and RNA and of u.v.-absorption spectra the nucleoprotein appears to have lost approx. 60% of the structural RNA origin...
متن کاملEffect of ribonuclease T1 on ribosomal subunits of rat liver.
The accessibility of 28S RNA within the ribosomal subunits to ribonuclease T1 was studied, in comparing results obtained after enzyme treatment of compact, K+ deficient 60S subunits and of EDTA-treated 60S subunits. RNA, extracted from the subunits, using a mixture of sodium dodecyl sulfate and phenol was analyzed on sucrose gradients. The RNA from active subunits was only degraded in high enzy...
متن کاملStudies on the Antigenic Structure of Ribonuclease
Alkali-denatured bovine pancreatic ribonuclease (RNase) reacts poorly with antibody to the native molecule, and RNase whose disulfide bridges have been broken by oxidation or reduction is completely inactive with this antiserum. These observations suggest that the antigenicity of the native protein is, in part, attributable to its conformation (1). Oxidized RNase has no detectable immunogenic o...
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ژورنال
عنوان ژورنال: Nippon kagaku zassi
سال: 1966
ISSN: 0369-5387,2185-0917
DOI: 10.1246/nikkashi1948.87.9_909