Abstract
5.8 S RNA-protein complexes were prepared using purified yeast 5.8 S RNA and proteins from the large ribosomal subunit of rat liver. Formation of such hybrid complexes, as measured by Miffipore filtration, was dependent on protein concentration. Binding of proteins to the RNA could approach saturation. Such complexes were isolated from sucrose density gradient centrifugation and shown to contain proteins L6, L8, L19, L35 and L35a. These proteins were identified by their molecular weights on polyacrylamide gels containing dodecylsulfate and their mobilities on two dimensional polyacrylamide gels.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2199-2207 |
| Number of pages | 9 |
| Journal | Nucleic Acids Research |
| Volume | 10 |
| Issue number | 7 |
| DOIs | |
| State | Published - Apr 10 1982 |
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ASJC Scopus subject areas
- Statistics, Probability and Uncertainty
- Applied Mathematics
- Health, Toxicology and Mutagenesis
- Toxicology
- Genetics(clinical)
- Genetics
Cite this
Binding of rat ribosomal proteins to yeast 5.8S ribosomal ribonucleic acid. / Lee, John C.; Henry, Beth.
In: Nucleic Acids Research, Vol. 10, No. 7, 10.04.1982, p. 2199-2207.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Binding of rat ribosomal proteins to yeast 5.8S ribosomal ribonucleic acid
AU - Lee, John C.
AU - Henry, Beth
PY - 1982/4/10
Y1 - 1982/4/10
N2 - 5.8 S RNA-protein complexes were prepared using purified yeast 5.8 S RNA and proteins from the large ribosomal subunit of rat liver. Formation of such hybrid complexes, as measured by Miffipore filtration, was dependent on protein concentration. Binding of proteins to the RNA could approach saturation. Such complexes were isolated from sucrose density gradient centrifugation and shown to contain proteins L6, L8, L19, L35 and L35a. These proteins were identified by their molecular weights on polyacrylamide gels containing dodecylsulfate and their mobilities on two dimensional polyacrylamide gels.
AB - 5.8 S RNA-protein complexes were prepared using purified yeast 5.8 S RNA and proteins from the large ribosomal subunit of rat liver. Formation of such hybrid complexes, as measured by Miffipore filtration, was dependent on protein concentration. Binding of proteins to the RNA could approach saturation. Such complexes were isolated from sucrose density gradient centrifugation and shown to contain proteins L6, L8, L19, L35 and L35a. These proteins were identified by their molecular weights on polyacrylamide gels containing dodecylsulfate and their mobilities on two dimensional polyacrylamide gels.
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UR - http://www.scopus.com/inward/citedby.url?scp=0020478921&partnerID=8YFLogxK
U2 - 10.1093/nar/10.7.2199
DO - 10.1093/nar/10.7.2199
M3 - Article
C2 - 7045808
AN - SCOPUS:0020478921
VL - 10
SP - 2199
EP - 2207
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 7
ER -