Characterization of Some of the Proteins of the Large Subunit of Rat Liver Ribosomes*

Biochemistry ◽  
1967 ◽  
Vol 6 (8) ◽  
pp. 2585-2591 ◽  
Author(s):  
Mary G. Hamilton ◽  
Mary E. Ruth
Keyword(s):  
Rat Liver ◽  
Large Subunit ◽  
Liver Ribosomes

scholarly journals ELECTRON MICROSCOPIC OBSERVATIONS ON THE LARGE SUBUNIT OF THE RAT LIVER RIBOSOME

1970 ◽  
Vol 47 (1) ◽  
pp. 211-221 ◽  
Author(s):  
J. Y. Haga ◽  
M. G. Hamilton ◽  
M. L. Petermann
Keyword(s):  
Rat Liver ◽  
Large Subunit ◽  
Sedimentation Coefficient ◽  
5S Rna ◽  
Frictional Drag ◽  
Electron Microscopic ◽  
Urea Treatment ◽  
Shadow Cast ◽  
Uranyl Oxalate ◽  
Liver Ribosomes

Active large subunits obtained by urea treatment of rat liver ribosomes, 59S, were compared with large subunits in intact ribosomes and with the 50S subunits obtained by EDTA treatment. For electron microscopy the specimens were negatively stained or shadow cast. The negatively stained 59S subunits had a slightly ovoidal form; their average dimensions, 244 ± 17 x 207 ± 18 A, were very close to the dimensions of the large subunits in intact ribosomes, and lay between the theoretical dimensions for anhydrous and fully hydrated particles that were calculated from the physical properties of the subunits in solution. The shadow-cast preparations showed particles of similar shape. The 50S subunits, which had lost their 5S RNA, were shadow cast at the same time. They appeared to be more spread out than the 59S subunits and had threadlike extensions. In the positively stained regions of uranyl oxalate-stained preparations the 50S particles varied greatly in shape and size, with average dimensions of 330 ± 21 x 276 ± 33 A, and showed threadlike extensions like those of the shadow-cast particles. For 50S particles in solution the frictional drag of these extensions probably accounts for their low sedimentation coefficient.

Charakterisierung von Proteinen aus Leber- und Hepatom-Ribosomen durch Polyacrylamid-Gelelektrophorese

1968 ◽  
Vol 23 (5) ◽  
pp. 690-694 ◽  
Author(s):  
H. Welfle ◽  
H. Bielka
Keyword(s):  
Rat Liver ◽  
Large Subunit ◽  
Small Subunit ◽  
Polyacrylamide Gel ◽  
Total Proteins ◽  
Acidic Proteins ◽  
Liver Ribosomes

Proteins isolated with 2 M LiCl from purified rat liver ribosomes can be separated electrophoretically on polyacrylamide gel into 24 fractions moving cationically at pH 2. In the proteins from crude ribosomal preparations, some bands of acidic proteins are additionally present. These acidic proteins can be removed by washing or by precipitation with MgCl2, corresponding to a loss of total proteins of about 5 — 10%, without impairing the proteosynthetic activity of the ribosomes.The proteins of the large subunit are also separated into 24 bands which are qualitatively identical to those of the 80 S-ribosomes. Only 18 bands, however, are found in the proteins from the small subunit.Proteins from hepatoma ribosomes and their subunits do not differ from those isolated from liver ribosomes.

Theileria parva ribosomal internal transcribed spacer sequences exhibit extensive polymorphism and mosaic evolution: application to the characterization of parasites from cattle and buffalo

Parasitology ◽  
1999 ◽  
Vol 118 (6) ◽  
pp. 541-551 ◽  
Author(s):  
N. E. COLLINS ◽  
B. A. ALLSOPP
Keyword(s):  
Genetic Recombination ◽  
Large Subunit ◽  
Small Subunit ◽  
Internal Transcribed Spacers ◽  
Rrna Genes ◽  
Gene Pools ◽  
Theileria Parva ◽  
Causative Agents ◽  
Internal Transcribed Spacer Sequences

We sequenced the rRNA genes and internal transcribed spacers (ITS) of several Theileria parva isolates in an attempt to distinguish between the causative agents of East coast fever and Corridor disease. The small subunit (SSU) and large subunit (LSU) rRNA genes from a cloned T. p. lawrencei parasite were sequenced; the former was identical to that of T. p. parva Muguga, and there were minor heterogeneities in the latter. The 5·8S gene sequences of 11 T. parva isolates were identical, but major differences were found in the ITS. Six characterization oligonucleotides were designed to hybridize within the variable ITS1 region; 93·5% of T. p. parva isolates examined were detected by probe TPP1 and 81·8% of T. p. lawrencei isolates were detected by TPL2 and/or TPL3a. There was no absolute distinction between T. p. parva and T. p. lawrencei and the former hybridized with fewer of the probes than did the latter. It therefore seems that a relatively homogenous subpopulation of T. parva has been selected in cattle from a more diverse gene pool in buffalo. The ITSs of both T. p. parva and T. p. lawrencei contained different combinations of identifiable sequence segments, resulting in a mosaic of segments in any one isolate, suggesting that the two populations undergo genetic recombination and that their gene pools are not completely separate.

scholarly journals Isolation and characterization of a mannan-binding protein from rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4247-4252
Author(s):  
Y. Mizuno ◽  
Y. Kozutsumi ◽  
T. Kawasaki ◽  
I. Yamashina
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Isolation And Characterization

scholarly journals Binding of Purified Antialbumin by Rat Liver Ribosomes

1965 ◽  
Vol 240 (7) ◽  
pp. 3009-3015 ◽  
Author(s):  
William A. Warren ◽  
Theodore Peters
Keyword(s):  
Rat Liver ◽  
Liver Ribosomes

scholarly journals Purification and partial characterization of 3-hydroxyisobutyryl-coenzyme A hydrolase of rat liver.

1994 ◽  
Vol 269 (19) ◽  
pp. 14248-14253
Author(s):  
Y. Shimomura ◽  
T. Murakami ◽  
N. Fujitsuka ◽  
N. Nakai ◽  
Y. Sato ◽  
...  
Keyword(s):  
Rat Liver ◽  
Coenzyme A ◽  
Partial Characterization
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