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.

Acid phosphatase activity of six ectomycorrhizal fungi

1979 ◽  
Vol 57 (11) ◽  
pp. 1203-1205 ◽  
Author(s):  
Iwan Ho ◽  
Bratislav Zak
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Ectomycorrhizal Fungi ◽  
Acid Phosphatase Activity ◽  
Test Methods ◽  
Starch Gel Electrophoresis ◽  
Tree Roots ◽  
Nitrophenyl Phosphate ◽  
Starch Gel

Six ectomycorrhizal fungi commonly associated with Douglas-fir were tested in vitro for acid phosphatase activity by measuring the amount of p-nitrophenyl phosphate converted to p-nitrophenol and by examining their production of isoenzymes detectable by starch gel electrophoresis. Both test methods showed acid phosphatase activity to be highest in Hebeloma crustuliniforme, followed by progressively lower activity in Laccaria laccata, Amanita muscaria, and Thelephora terrestris. Rhizopogon vinicolor and Piloderma bicolor showed low activity. We discuss the significance of these fungi in the utilization of complex phosphates by tree roots.

EFFECTS OF 5α-ANDROSTANE-3β,17β-DIOL AND 5β-DIHYDROTESTOSTERONE ON ACID PHOSPHATASE ACTIVITY IN THE PROSTATE GLAND OF THE CASTRATED ADULT RAT

1978 ◽  
Vol 79 (1) ◽  
pp. 9-16 ◽  
Author(s):  
M. P. TENNISWOOD ◽  
PAMELA P. ABRAHAMS ◽  
C. E. BIRD ◽  
A. F. CLARK
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Prostate Gland ◽  
Intraperitoneal Administration ◽  
Adult Rat ◽  
Secretory Acid Phosphatase

Polyacrylamide gel electrophoresis of filtrates from adult rat prostatic tissue showed two bands of acid phosphatase activity. These corresponded to the lysosomal and secretory acid phosphatases. After castration the secretory acid phosphatase disappeared. The specific activity of the enzyme increased from the time of castration to a maximum on day 7 before declining steadily, while the percentage inhibition by tartrate of acid phosphatase increased from control levels to a maximum on day 7 and then decreased to a new steady state by day 15. When 5α-androstane-3β,17β-diol was administered i.p. at a dose of 2 mg/day, starting immediately after castration, the secretory acid phosphatase was retained but the percentage inhibition and the specific activity were both raised above control levels. When this steroid was administered daily starting 7 days after castration the secretory acid phosphatase band on the gels returned more rapidly than with the classical androgens, but the percentage inhibition and specific activity were once again raised. Intraperitoneal administration of 5β-dihydrotestosterone, at a dose of 2 mg/day, did not maintain the secretory acid phosphatase activity which disappeared by day 5. However, the specific activity of acid phosphatase and the percentage inhibition by tartrate were both raised throughout the experiment. If this steroid was given 7 days after castration, the percentage inhibition by tartrate did not respond and fell to the level seen in castrated rats. The specific activity, however, remained significantly above the level found in castrated control rats.

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.

scholarly journals The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

scholarly journals Acrylamide gel electrophoresis of proteins, acid phosphatases and RN-ases from three potato varieties

2015 ◽  
Vol 41 (1) ◽  
pp. 107-112 ◽  
Author(s):  
A. Kubicz ◽  
E. Wieczorek ◽  
B. Morawiecka
Keyword(s):  
Solanum Tuberosum ◽  
Acid Phosphatase ◽  
Relative Abundance ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Disc Electrophoresis ◽  
Acid Phosphatases ◽  
Main Zone ◽  
Activity Distribution ◽  
Electrophoresis Of Proteins

Studies on variety differences in the protein and acid phosphatase patterns as well as ribunuclease activity distribution were carried out by disc electrophoresis on saline extracts of three varieties of the potato <i>Solanum tuberosum</i> (L.). The protein bands varied in number, position and relative abundance. One main zone of the acid phosphatase activity was detected consisting of 2-3 electrophoretically different bands. Variety differences were concerned with the number and relative abundance of these bands. RNase activity was detected in 4 main zones, in some of them additional subbands were visible. Differences between the three examined varieties were reflected in the occurence of the particular activity zones or their subbands.

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