scholarly journals Multiple forms of rat kidney mutarotase.

1976 ◽  
Vol 24 (11) ◽  
pp. 2893-2895 ◽  
Author(s):  
JUN OKUDA ◽  
ICHITOMO MIWA ◽  
YUKIYASU TOYODA
Keyword(s):  
Rat Kidney ◽  
Multiple Forms

scholarly journals The distribution of some hydrolases in glomeruli and tubular fragments prepared from rat kidney by zonal centrifugation

1971 ◽  
Vol 122 (5) ◽  
pp. 641-645 ◽  
Author(s):  
D. G. Taylor ◽  
R. G. Price ◽  
D. Robinson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Starch Gel Electrophoresis ◽  
Multiple Forms ◽  
Rat Kidney Cortex ◽  
Starch Gel

1. A collagenase digest of rat kidney cortex was separated into four bands by zonal centrifugation. 2. Two of these bands were shown by light-microscopy to contain glomeruli and tubular fragments, which were free from each other and well separated from other renal material. 3. Protein, N-acetyl-β-glucosaminidase, 5′-nucleotidase, l-leucine β-naphthylamidase, leucine aminopeptidase, acid phosphatase and alkaline phosphatase were assayed across the gradient. 4. The greater proportion of these enzyme activities was recovered in the tubular fragments and acid phosphatase was the only enzyme detected in significant amounts in the glomeruli. 5. Tubular fragments and glomeruli were sedimented and multiple forms of β-naphthylamidase, N-acetyl-β-glucosaminidase, acid phosphatase and alkaline phosphatase were investigated by starch-gel electrophoresis.

scholarly journals Tissue distribution and subunit structures of the multiple forms of glutathione S-transferase in the rat

1981 ◽  
Vol 193 (1) ◽  
pp. 367-370 ◽  
Author(s):  
N C Scully ◽  
T J Mantle
Keyword(s):  
Tissue Distribution ◽  
Rat Kidney ◽  
Multiple Forms ◽  
Glutathione S Transferase

A study of the subunit structures of the multiple forms of glutathione S-transferase in rat kidney, testis, lung and spleen is shown to be consistent with a proteolytic model for the generation of the multiple forms.

The Existence of Multiple Forms of Rat Kidney Transamidinase

Guanidines 2 ◽  
1989 ◽  
pp. 61-69
Author(s):  
Myron D. Gross ◽  
Alexander M. Simon ◽  
Richard J. Jenny ◽  
Ernest D. Gray ◽  
Denise M. McGuire ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Multiple Forms

Multiple Forms of Rat Kidney L-Arginine:Glycine Amidinotransferase

1988 ◽  
Vol 118 (11) ◽  
pp. 1403-1409 ◽  
Author(s):  
Myron D. Gross ◽  
Alexander M. Simon ◽  
Richard J. Jenny ◽  
Ernest D. Gray ◽  
Denise M. McGuire ◽  
...  
Keyword(s):  
Rat Kidney ◽  
Multiple Forms

scholarly journals The cellular distribution of some rat-kidney glycosidases

1967 ◽  
Vol 105 (2) ◽  
pp. 877-883 ◽  
Author(s):  
R. G. Price ◽  
N. Dance
Keyword(s):  
Microsomal Fraction ◽  
Soluble Fraction ◽  
Rat Kidney ◽  
Significant Proportion ◽  
Cellular Distribution ◽  
Galactosidase Activity ◽  
Marker Enzymes ◽  
Multiple Forms ◽  
Latent Form ◽  
Starch Gel

1. Free and total activities of β-glucosidase, β-galactosidase, N-acetyl-β-glucosaminidase and β-glucuronidase have been determined fluorimetrically in five subcellular fractions of rat kidney. 2. The β-glucosidase activity appeared in the soluble fraction, β-glucuronidase had the distribution pattern of a lysosomal enzyme, and both β-galactosidase and N-acetyl-β-glucosaminidase had bimodal distributions. 3. Two types of β-galactosidase activity were found: a sedimentable type, having optimum pH3·7, mol.wt. about 80000 and slow electrophoretic mobility at pH7·0 in starch gel; and a soluble type of much faster mobility, having optimum pH5·5–6·5 and mol.wt. about 40000. 4. Evidence is presented that the β-glucosidase and the soluble type of β-galactosidase are the same enzyme. 5. Most of the N-acetyl-β-glucosaminidase activity was in the lysosome-rich fractions, but a significant proportion occurred in the microsomal fraction in a non-latent form. 6. The use of β-galactosidase and N-acetyl-β-glucosaminidase as lysosomal marker enzymes is complicated by the possible presence of multiple forms, but this limitation does not apply to β-glucuronidase in the rat kidney.

A Comparison of Multiple Forms of Renin in Rat Renal Perfusate with those in Renal Extract

1980 ◽  
Vol 59 (s6) ◽  
pp. 37s-40s ◽  
Author(s):  
Haruyuki Nakane ◽  
Yoko Nakane ◽  
Jiro Misumi ◽  
Takao Saruta ◽  
Pierre Corvol ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Rat Kidney ◽  
Relative Proportion ◽  
Active Form ◽  
Low Molecular Weight ◽  
Multiple Forms ◽  
Isoelectric Points ◽  
Perfused Rat Kidney ◽  
Inactive Renin

1. Physicochemical properties of renin secreted by isolated perfused rat kidney were examined and the results compared with those obtained for the renin in renal extract. 2. In renal extract, two high-molecular-weight reruns (molecular weight 65 000 and 55 000) and one low-molecular-weight renin (molecular weight 39 000) were found. Their relative proportion varied depending on extraction conditions. By acidification, high-molecular-weight renins were converted into low-molecular-weight renin without marked changes in activity. 3. In renal perfusate only low-molecular-weight renin was found after renin stimulation by isoprenaline or anoxia. Inactive renin was not found. 4. Renin in renal extract and perfusate samples were both found to consist of at least four isoenzymes having different isoelectric points (pI). The pI patterns were identical in renal extract and perfusate samples: pI 5.7 (60-70%), 5.5 (15-25%), 5.3 (5-10%) and 5.0-5.2 (2-5%). 5. These results indicate that the native renin secreted by rat kidney consists entirely of the low-molecular-weight and active form comprising multiple isoenzymes with a stable pI pattern.

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.

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