Identification of Multiple forms of the Cytosolic 5′-Nucleotidase/Phosphotransferase in Rat Tissues

1998 ◽  
pp. 495-499 ◽  
Author(s):  
R. Pesi ◽  
S. Allegrini ◽  
S. Golfarini ◽  
C. Baiocchi ◽  
E. Moretti ◽  
...  
Keyword(s):  
Rat Tissues ◽  
Multiple Forms

Multiple forms of phosphofrugtokinase in rat tissues

1974 ◽  
Vol 5 (1) ◽  
pp. 89-93 ◽  
Author(s):  
W. Kirby ◽  
C.B. Taylor
Keyword(s):  
Rat Tissues ◽  
Multiple Forms

Multiple forms of angiotensin II receptors in rat tissues

1991 ◽  
Vol 7 (1) ◽  
pp. 21-26 ◽  
Author(s):  
E. Jimenez ◽  
S. Marsigliante ◽  
S. Barker ◽  
J. P. Hinson ◽  
G. P. Vinson
Keyword(s):  
Angiotensin Ii ◽  
Specific Binding ◽  
Zona Glomerulosa ◽  
Rat Tissues ◽  
Multiple Forms ◽  
High Affinity ◽  
Receptor Isoforms ◽  
Isoelectric Points ◽  
Liver Membranes ◽  
Rat Tissue

ABSTRACT Angiotensin II (AII) receptors were identified in rat tissue membranes by specific binding of 125I-labelled AII. Using an isoelectric focusing technique, two forms of the high-affinity AII receptor were identified in rat adrenal zona glomerulosa and liver membranes. These migrated to isoelectric points (pI) 6.8 and 6.7. Two low-affinity forms migrated to pI 6.5 and 6.3. The two high-affinity forms were in greatest abundance in the zona glomerulosa, while the low-affinity pI 6.5 isoform was predominant in liver membranes. In uterine membranes both low-affinity isoforms were observed, but there was only one of the high-affinity forms (pI 6.7). Concentrations of AII receptor isoforms were increased in the zona glomerulosa of sodium-deprived rats. Reduction of disulphide bridges with dithiothreitol (DTT) had different effects on the various AII receptor isoforms. Thus 1 mmol DTT/l caused a twofold increase in 125I-labelled AII binding in zona glomerulosa membranes. DTT produced no appreciable differences in specific AII binding in uterine membranes, whereas there was a 50% reduction of binding in liver membranes. At 20mmol/1, DTT greatly decreased AII binding in all tissues. The data suggest the existence of multiple forms of AII receptors which may have different functions.

Multiple forms of AMP deaminase in various rat tissues

FEBS Letters ◽  
1974 ◽  
Vol 44 (1) ◽  
pp. 63-66 ◽  
Author(s):  
N. Ogasawara ◽  
H. Goto ◽  
T. Watanabe
Keyword(s):  
Rat Tissues ◽  
Amp Deaminase ◽  
Multiple Forms

Multiple forms of elongation factor 1 in various rat tissues

1975 ◽  
Vol 166 (2) ◽  
pp. 683-684 ◽  
Author(s):  
Robert Bolla ◽  
Herbert Weissbach ◽  
Nathan Brot
Keyword(s):  
Elongation Factor ◽  
Rat Tissues ◽  
Multiple Forms ◽  
Elongation Factor 1

scholarly journals Specificity and multiple forms of β-galactosidase in the rat

1965 ◽  
Vol 97 (1) ◽  
pp. 59-66 ◽  
Author(s):  
AJ Furth ◽  
D Robinson
Keyword(s):  
Liver Enzyme ◽  
Cellular Localization ◽  
Deae Cellulose ◽  
Rat Tissues ◽  
Multiple Forms ◽  
Chromatographic Pattern ◽  
Beta Glucosidase ◽  
Inhibition Studies ◽  
Non Destructive ◽  
Beta Galactosidase

1. Ten rat tissues and organs have been assayed for beta-galactosidase with phenyl beta-d-galactoside, p-nitrophenyl beta-d-galactoside, p-aminophenyl beta-d-galactoside and 4-methylumbelliferyl beta-d-galactoside as substrates. 2. The relative activities of these tissues are independent of the mode of assay, and maximum rates of hydrolysis are not greatly affected by the nature of the substrate. 3. Inhibition studies suggest the liver enzyme has no associated beta-glucosidase activity. 4. There is no cellular localization of preferential activity towards any of the four substrates in liver, kidney or spleen. 5. Evidence suggesting the non-destructive penetration of liver lysosomal membranes by p-nitrophenyl beta-d-galactoside is presented. 6. Liver lysosomal beta-galactosidase exists in multiple forms that can be separated on DEAE-cellulose, and the enzyme components that are bound to the membrane appear to be similar to those of the lysosome sap. 7. The chromatographic pattern of enzyme excreted in the urine is compared with those from the kidney, intestine, spleen and liver.

Identification of multiple forms of cytosolic 5′-nucleotidase phosphotransferase in rat tissues

1997 ◽  
Vol 30 (3) ◽  
pp. 287
Author(s):  
R. Pesi ◽  
S. Allegrini ◽  
S. Golfarini ◽  
C. Baiocchi ◽  
E. Moretti ◽  
...  
Keyword(s):  
Rat Tissues ◽  
Multiple Forms

Multiple forms of phosphofructokinase in rat tissues and rat tumors

1972 ◽  
Vol 48 (3) ◽  
pp. 473-479 ◽  
Author(s):  
Norimasa Kurata ◽  
Taijiro Matsushima ◽  
Takashi Sugimura
Keyword(s):  
Rat Tissues ◽  
Multiple Forms ◽  
Rat Tumors

Identifying suboptimalities with factorial model comparison

2018 ◽  
Vol 41 ◽  
Author(s):  
Wei Ji Ma
Keyword(s):  
Experimental Design ◽  
Model Comparison ◽  
Process Models ◽  
Multiple Forms ◽  
Factorial Experimental Design ◽  
Factorial Model ◽  
Multiple Components ◽  
The Many

AbstractGiven the many types of suboptimality in perception, I ask how one should test for multiple forms of suboptimality at the same time – or, more generally, how one should compare process models that can differ in any or all of the multiple components. In analogy to factorial experimental design, I advocate for factorial model comparison.

High-resolution scanning electron microscopy (HRSEM) of mitochondria from various rat tissues

1988 ◽  
Vol 46 ◽  
pp. 14-15
Author(s):  
P.J. Lea ◽  
M.J. Hollenberg
Keyword(s):  
Electron Microscopy ◽  
Pigment Epithelium ◽  
Retinal Pigment ◽  
Rat Hepatocytes ◽  
Three Dimensions ◽  
Objective Lens ◽  
Rat Tissues ◽  
Thin Sections ◽  
Reconstruction Methods ◽  
Scanning Electron

Our current understanding of mitochondrial ultrastructure has been derived primarily from thin sections using transmission electron microscopy (TEM). This information has been extrapolated into three dimensions by artist's impressions (1) or serial sectioning techniques in combination with computer processing (2). The resolution of serial reconstruction methods is limited by section thickness whereas artist's impressions have obvious disadvantages.In contrast, the new techniques of HRSEM used in this study (3) offer the opportunity to view simultaneously both the internal and external structure of mitochondria directly in three dimensions and in detail.The tridimensional ultrastructure of mitochondria from rat hepatocytes, retinal (retinal pigment epithelium), renal (proximal convoluted tubule) and adrenal cortex cells were studied by HRSEM. The specimens were prepared by aldehyde-osmium fixation in combination with freeze cleavage followed by partial extraction of cytosol with a weak solution of osmium tetroxide (4). The specimens were examined with a Hitachi S-570 scanning electron microscope, resolution better than 30 nm, where the secondary electron detector is located in the column directly above the specimen inserted within the objective lens.

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