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

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.

Biochemistry ◽  
1967 ◽  
Vol 6 (8) ◽  
pp. 2585-2591 ◽  
Author(s):  
Mary G. Hamilton ◽  
Mary E. Ruth

1968 ◽  
Vol 106 (1) ◽  
pp. 263-266 ◽  
Author(s):  
R. Brentani ◽  
M. Brentani ◽  
I. Raw ◽  
J. L. M. Cunha ◽  
N. Wrotschincky

1. Rat-liver ribosomes lose about 50% of their amino acid-incorporating activity when preincubated with ribonuclease. 2. This preincubation results also in loss of about 50% of the original protein content and 75% of the RNA. 3. Ribosomes sedimented by ultracentrifugation, after preincubation with ribonuclease, show negligible contamination by crystalline enzyme. 4. Washing of ribosomes treated with ribonuclease releases further protein, restoring the original RNA/protein ratio. 5. The washed particle is again capable of promoting amino acid incorporation. 6. Examination of ribosomes treated with ribonuclease in the analytical ultracentrifuge reveals destruction of ribosomes, disappearance of dimers and a decrease in the sedimentation coefficient of monomers. 7. Washed ribosomes consist of even smaller particles with a sedimentation coefficient 60s.


1982 ◽  
Vol 91 (1) ◽  
pp. 363-367 ◽  
Author(s):  
Kazue AOYAMA ◽  
Soh HIDAKA ◽  
Tatsuo TANAKA ◽  
Kiichi ISHIKAWA

1968 ◽  
Vol 23 (5) ◽  
pp. 690-694 ◽  
Author(s):  
H. Welfle ◽  
H. Bielka

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.


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

1981 ◽  
Vol 184 (3) ◽  
pp. 551-556 ◽  
Author(s):  
Steven Fabijanski ◽  
Maria Pellegrini

1968 ◽  
Vol 243 (1) ◽  
pp. 192-199 ◽  
Author(s):  
Jacqueline J. Bungenberg de Jong ◽  
Julian B. Marsh

2005 ◽  
Vol 289 (2) ◽  
pp. C372-C378 ◽  
Author(s):  
Roberto Justo ◽  
Jordi Boada ◽  
Margalida Frontera ◽  
Jordi Oliver ◽  
Jordi Bermúdez ◽  
...  

In the present study, we have investigated gender differences in rat liver mitochondrial oxidative metabolism. Total mitochondrial population (M) as well as the heavy (M1), medium (M3), and light (M8) mitochondrial fractions obtained by means of differential centrifugation steps at 1,000, 3,000, and 8,000 g, respectively, were isolated. Electron microscopic analysis was performed and mitochondrial protein content and cardiolipin levels, mitochondrial O2 flux, ATP synthase activity, mitochondrial membrane potential, and mitochondrial transcription factor A (TFAM) protein levels were measured in each sample. Our results indicate that mitochondria from females have higher protein content and higher cardiolipin levels, greater respiratory and phosphorylative capacities, and more-energized mitochondria in respiratory state 3. Moreover, protein levels of TFAM were four times greater in females than in males. Gender differences in the aforementioned parameters were more patent in the isolated heavy M1 and M3 mitochondrial fractions. The present study demonstrates that gender-related differences in liver mitochondrial function are due mainly to a higher capacity and efficiency of substrate oxidation, likely related to greater mitochondrial machinery in females than in males, which is in accord with greater mitochondrial differentiation in females.


Biochemistry ◽  
1972 ◽  
Vol 11 (12) ◽  
pp. 2323-2326 ◽  
Author(s):  
Mary L. Petermann ◽  
Mary G. Hamilton ◽  
Amalia Pavlovec

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