|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|5131704||1378766||2017||3 صفحه PDF||سفارش دهید||دانلود کنید|
- S1 is removed from ribosomes by centrifugation following incubation with poly(C) or poly(U).
- Size matters: Optimally, the pyrimidine polyribonucleotide is 100-200Â nt long.
- The treatment is compatible with standard ribosome washing procedures.
- The expensive affinity resin is no longer needed.
The paper reports an inexpensive and efficient procedure for the removal of protein S1 from E.Â coli ribosomes. It comprises incubation of ribosomes in a pyrimidine polyribonucleotide solution followed by centrifugation of the sample through a sucrose cushion. To avoid co-sedimentation of the S1-bound polypyrimidine with the ribosomes, its length should not exceed several hundred nucleotides. Unlike popular affinity chromatography through a poly(U) Sepharose or poly(U) cellulose column, the method tolerates limited polyribonucleotide degradation by eventual traces of ribonucleases, and can readily be incorporated into standard protocols for the isolation of ribosomes by centrifugation.
Journal: Analytical Biochemistry - Volume 517, 15 January 2017, Pages 53-55