Recombinant rat liver guanidinoacetate methyltransferase: reactivity and function of sulfhydryl groups

Biochemistry ◽  
1988 ◽  
Vol 27 (20) ◽  
pp. 7658-7664 ◽  
Author(s):  
Motoji Fujioka ◽  
Kiyoshi Konishi ◽  
Yoshimi Takata
Keyword(s):  
Rat Liver ◽  
Sulfhydryl Groups ◽  
And Function

scholarly journals Differences in size, structure and function of free and membrane-bound polyribosomes of rat liver. Evidence for a single class of membrane-bound polyribosomes

1977 ◽  
Vol 168 (1) ◽  
pp. 1-8 ◽  
Author(s):  
J C Ramsey ◽  
W J Steele
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Size Structure ◽  
Large Fraction ◽  
Liver Homogenate ◽  
Structure And Function ◽  
Structural And Functional Properties ◽  
Membrane Bound ◽  
And Function

Free loosely bound and tightly bound polyribosomes were separated from rat liver homogenate by salt extraction followed by differential centrifugation, and several of their structural and functional properties were compared to resolve the existence of loosely bound polyribosomes and verify the specificity of the separation. The free and loosely bound polyribosomes have similar sedimentation profiles and polyribosome contents, their subunit proteins have similar electrophoretic patterns and their products of protein synthesis in vitro show a close correspondence in size and amounts synthesized. In contrast, the tightly bound polyribosomes have different properties from those of the free and loosely bound polyribosomes; their average size is significantly smaller; their polyribosome content is higher; their 60 S-subunit proteins lack two components and contain four or more components not found elsewhere; their products of protein synthesis in vitro differ in size and amounts synthesized. These observations show that rat liver membranes entrap a large fraction of the free polyribosomes at low salt concentrations and that these polyribosomes are similar to those of the free-polyribosome fraction and are different from those of the tightly bound polyribosome fraction in size, structure and function.

Down-regulation of expression and function of the rat liver Na+/bile acid cotransporter in extrahepatic cholestasis

1996 ◽  
Vol 110 (1) ◽  
pp. 199-209 ◽  
Author(s):  
C Gartung ◽  
M Ananthanarayanan ◽  
MA Rahman ◽  
S Schuele ◽  
S Nundy ◽  
...  
Keyword(s):  
Bile Acid ◽  
Rat Liver ◽  
Down Regulation ◽  
Regulation Of Expression ◽  
Extrahepatic Cholestasis ◽  
And Function

Effects of Alkyl Alcohols and Related Chemicals on Rat Liver Structure and Function

1991 ◽  
Vol 41 (6) ◽  
pp. 405-413
Author(s):  
Takashi Wakabayashi ◽  
Kayo Adachi ◽  
Jerzy Popinigis
Keyword(s):  
Rat Liver ◽  
Structure And Function ◽  
Liver Structure ◽  
And Function

scholarly journals Expression Profile and Function Analysis of LncRNAs during Priming Phase of Rat Liver Regeneration

PLoS ONE ◽  
2016 ◽  
Vol 11 (6) ◽  
pp. e0156128 ◽  
Author(s):  
Jun Li ◽  
Wei Jin ◽  
Yanli Qin ◽  
Weiming Zhao ◽  
Cuifang Chang ◽  
...  
Keyword(s):  
Liver Regeneration ◽  
Rat Liver ◽  
Expression Profile ◽  
Function Analysis ◽  
Rat Liver Regeneration ◽  
Priming Phase ◽  
And Function

Comparison of the structure and function of ribulosebisphosphate carboxylase–oxygenase from a cold-hardy and nonhardy potato species

1981 ◽  
Vol 59 (4) ◽  
pp. 280-289 ◽  
Author(s):  
Norman P. A. Huner ◽  
Jiwan P. Palta ◽  
Paul H. Li ◽  
John V. Carter
Keyword(s):  
Large Subunit ◽  
Structure And Function ◽  
Sulfhydryl Groups ◽  
Relative Mass ◽  
Nitrobenzoic Acid ◽  
Significant Difference ◽  
Ribulosebisphosphate Carboxylase ◽  
Cold Hardy ◽  
And Function ◽  
Kinetics Of

A comparison of ribulosebisphosphate carboxylase–oxygenase from the leaves of the non-acclimated, cold-hardy species, Solanum commersonii, and the nonacclimated, nonhardy species, Solanum tuberosum showed that this enzyme from the two species differed in structure and function. The results of sulfhydryl group titration with 5,5′-dithiobis(2-nitrobenzoic acid) indicated that the kinetics of titration and the number of accessible sulfhydryl groups in the native enzymes were different. After 30 min, the enzyme from the hardy species had 1.7 times fewer sulfhydryl groups titrated than that from the nonhardy species. In the presence of 1% (w/v) sodium dodecyl sulfate, the total number of sulfhydryl groups titratable with 5,5′-dithiobis-(2-nitrobenzoic acid) was the same for both species. However, this denaturant had a differential effect on the kinetics of titration with 5,5′-dithiobis(2-nitrobenzoic acid). Both enzymes had a native molecular weight of about 550 000. The quaternary structures of the two enzymes were similar with the presence of large and small subunits of 54 000 and 14 000, respectively. However, there was more polypeptide of 108 000 – 110 000 present in preparations of the enzyme from S. tuberosum than from S. commersonii. This polypeptide is an apparent dimer of the large subunit on a relative mass basis. The large subunit of the enzyme from S. tuberosum was more sensitive to the absence of reducing agent and was more sensitive to freezing and thawing than the large subunit of the enzyme from S. commersonii. Catalytic properties of both enzymes at 5 and 25 °C indicated no significant difference in the [Formula: see text] at either temperature. However, the Vmax at 5 °C for the enzyme from S. commersonii was 35% higher than that of the enzyme from S. tuberosum. In contrast, the Vmax at 25 °C for the enzyme of the hardy species was 250% lower than that of the enzyme from the nonhardy species.

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