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.

Ultracytochemical Localization of Aryl Sulfatase, Esterase, and Acid and Alkaline Phosphatases with 4-Nitrocatechol Substrates and Tetrazolium Salts

1974 ◽  
Vol 32 ◽  
pp. 226-227
Author(s):  
W. Allen Shannon ◽  
Yoshinobu Hoshino ◽  
Hannah L. Wasserkrug ◽  
Arnold M. Seligman
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Alkaline Phosphatases ◽  
Cytochemical Localization ◽  
Rat Kidney Cortex ◽  
Aryl Sulfatase ◽  
Tetrazolium Salts

The ultra cytochemical localization of various hydrolases, i. e, aryl sulfatase(ArS), esterase (Est), acid phosphatase(AcP) and alkaline phosphatase (A1P) is demonstrated in rat kidney cortex with newly developed 4-nitrocatechol substrates (2-hydroxy-5-nitrophenyl compounds) (Fig. 1) and tetrazolium salts, Nitro-BT, BSPT, and BPPT. ArS was also investigated in adrenal cortex.

The Red Cell Acid Phosphatase Polymorphism in Greek b-Thalassemia Patients

1975 ◽  
Vol 24 (3-4) ◽  
pp. 337-338
Author(s):  
A. Kalos ◽  
K. Melissinos ◽  
A. Archimandritis ◽  
G. Kourounis ◽  
B. Angelopoulos
Keyword(s):  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Red Cell ◽  
Gene Frequencies ◽  
Starch Gel ◽  
Acid Phosphatase Polymorphism ◽  
Cell Acid

Red cell acid phosphatase polymorphism was studied by starch gel electrophoresis in 70 b-thalassemia patients and in 310 healthy Greeks. Our results gave the following gene frequencies: b-thalassemia patients: pa 0.321, pb 0.643, pc 0.036; healthy Greeks: pa 0.302, pb 0.653, pc 0.045. No statistically significant differences were found between the two groups.

scholarly journals Identifying Olive Cultivars by Isozyme Analysis

1995 ◽  
Vol 120 (2) ◽  
pp. 318-324 ◽  
Author(s):  
Isabel Trujillo ◽  
Luis Rallo ◽  
Pere Arús
Keyword(s):  
Gel Electrophoresis ◽  
Malic Enzyme ◽  
Leucine Aminopeptidase ◽  
Morphological Characteristics ◽  
Starch Gel Electrophoresis ◽  
Banding Patterns ◽  
Glucose Phosphate ◽  
Olive Cultivars ◽  
Starch Gel ◽  
Different Origins

Pollen samples of 155 olive (Olea europaea L.) cultivars from different origins were analyzed to study isoenzymatic variability in five enzyme systems: alcohol dehydrogenase (ADH), esterase (EST), glucose phosphate isomerase (GPI), leucine aminopeptidase (LAP), and malic enzyme (ME) using starch gel electrophoresis. Polymorphism was observed in all of the isozyme systems. ME, GPI, EST, and LAP were the most useful systems for identification of cultivars. Different combinations of banding patterns of these systems allowed us to identify 85% of the cultivars. The remainder were separated into groups of two or three cultivars that could be identified using morphological characteristics. No intracultivar polymorphisms were observed.

GENETIC STUDIES OF ISOZYMES IN NEUROSPORA. I. A STUDY OF EIGHT SPECIES

1971 ◽  
Vol 13 (2) ◽  
pp. 298-305 ◽  
Author(s):  
M. Mohan Reddy ◽  
S. F. H. Threlkeld
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Starch Gel Electrophoresis ◽  
Acid Phosphatases ◽  
Genetic Studies ◽  
Starch Gel

Mycelial extracts of 34 strains representing eight species of the genus Neurospora were subjected to acrylamide and starch gel electrophoresis to detect sites of esterase, lactate dehydrogenase, amylase, peroxidase, and acid phosphatase activity. Nine isozymes of esterases, four isozymes of lactate dehyrogenases, three isozymes of peroxidases, and two isozymes of acid phosphatases were detected on the gels for the species. The application of zymograms as a biochemical means to characterize species is discussed.

Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1317-1320 ◽  
Author(s):  
E. kaminski ◽  
W. Bushuk
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Direct Detection ◽  
Proteolytic Enzymes ◽  
Urea Concentration ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Multiple Forms ◽  
Starch Gel ◽  
Sensitive Method

A rapid and sensitive method for the direct detection of multiple forms of proteolytic enzymes by starch gel electrophoresis is described. The location of the enzyme components is identified by the degradation of hemoglobin which is included in the starch gel. This method was used to identify the enzyme components of the 10 commercial proteolytic enzymes bromelain, chymotrypsin, ficin, papain, pepsin, pronase B, protease, proteinase, and two preparations of trypsin. The effects of urea concentration and the ionic strength of aluminium lactate buffer were also examined. The best results were obtained with 3 M urea and with an ionic strength of 0.1 for the lactate buffer. It was observed that the number of enzyme components decreased with increasing concentrations of urea or increasing ionic strength of lactate buffer. The number of enzyme components did not always correspond to the number of protein bands. Self-digestion occurred in some of the protein bands in the starch gel after electrophoretic separation of the proteolytic enzymes.

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