Abstract
A high molecular weight complex has been isolated from rat liver which contains all the aminoacyl-transfer RNA synthetases and and a large proportion of the tRNA present in the high-speed supernatant fraction. The complex could be partially purified by chromatography on Sephadex G200 and Sepharose 6B. The complex could be disrupted by excess homogenization and freezing and thawing with a concomitant decrease in the activities of the aminoacyl-tRNA synthetases. The results suggest that some of the presumed "soluble" components of the protein synthetic apparatus may be present in highly organized structures within the cell.
| Original language | English |
|---|---|
| Pages (from-to) | 113-122 |
| Number of pages | 10 |
| Journal | Journal of Molecular Biology |
| Volume | 60 |
| Issue number | 1 |
| DOIs | |
| State | Published - Aug 28 1971 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Virology
Cite this
Complex of aminoacyl-transfer RNA synthetases. / Bandyopadhyay, Alok Kumar; Deutscher, Murray P.
In: Journal of Molecular Biology, Vol. 60, No. 1, 28.08.1971, p. 113-122.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Complex of aminoacyl-transfer RNA synthetases
AU - Bandyopadhyay, Alok Kumar
AU - Deutscher, Murray P
PY - 1971/8/28
Y1 - 1971/8/28
N2 - A high molecular weight complex has been isolated from rat liver which contains all the aminoacyl-transfer RNA synthetases and and a large proportion of the tRNA present in the high-speed supernatant fraction. The complex could be partially purified by chromatography on Sephadex G200 and Sepharose 6B. The complex could be disrupted by excess homogenization and freezing and thawing with a concomitant decrease in the activities of the aminoacyl-tRNA synthetases. The results suggest that some of the presumed "soluble" components of the protein synthetic apparatus may be present in highly organized structures within the cell.
AB - A high molecular weight complex has been isolated from rat liver which contains all the aminoacyl-transfer RNA synthetases and and a large proportion of the tRNA present in the high-speed supernatant fraction. The complex could be partially purified by chromatography on Sephadex G200 and Sepharose 6B. The complex could be disrupted by excess homogenization and freezing and thawing with a concomitant decrease in the activities of the aminoacyl-tRNA synthetases. The results suggest that some of the presumed "soluble" components of the protein synthetic apparatus may be present in highly organized structures within the cell.
UR - http://www.scopus.com/inward/record.url?scp=0015243504&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0015243504&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(71)90451-7
DO - 10.1016/0022-2836(71)90451-7
M3 - Article
VL - 60
SP - 113
EP - 122
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -