The Simultaneous Identification of Seminal Acid Phosphatase and Phosphoglucomutase by Starch Gel Electrophoresis

1980 ◽  
Vol 25 (1) ◽  
pp. 10945J ◽  
Author(s):  
H. G. Linde ◽  
K. E. Molnar
Keyword(s):  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Simultaneous Identification

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 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.

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.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

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