scholarly journals The development of ribonuclease and acid phosphatase during germination of Pisum arvense

1974 ◽  
Vol 142 (2) ◽  
pp. 211-219 ◽  
Author(s):  
Geoffrey R. Barker ◽  
Clifford M. Bray ◽  
Trevor J. Walter
Keyword(s):  
Amino Acids ◽  
Acid Phosphatase ◽  
Phase I ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
De Novo ◽  
Deuterium Oxide ◽  
Buoyant Density ◽  
Ribonuclease Activity ◽  
Supernatant Fraction

1. Development of ribonuclease activity in the cotyledons of germinating peas is biphasic, the time of appearance of the two phases depending on the conditions of growth. 2. Acid phosphatase exhibits a single phase of development. 3. Cycloheximide inhibits development of ribonuclease activity in phase II but not in phase I. 4.14C-labelled amino acids are not incorporated into ribonuclease isolated during phase I. 5. The buoyant density of ribonuclease isolated during phase I is not affected by imbibition of the seed in 80% deuterium oxide. 6. Acid phosphatase was isolated from the supernatant fraction of the cotyledons of germinating peas and partially purified. 7. Development of acid phosphatase activity during germination is inhibited by treatment of the seed with cycloheximide or actinomycin D. 8. Partial purification of acid phosphatase from peas germinated in the presence of14C-labelled amino acids suggests that the enzyme is radioactively labelled. 9. Germination of peas in the presence of 80% deuterium oxide results in an increase in the buoyant density of acid phosphatase. 10. The results suggest that increase in ribonuclease activity during the first 4 days of germination does not result from synthesis of protein de novo, but that the corresponding increase in acid phosphatase activity does result from synthesis de novo.

Studies on Leukocyte Phosphatases. III. Inhibition of Leukocyte Acid Phosphatase by Zinc

1971 ◽  
Vol 17 (12) ◽  
pp. 1176-1179 ◽  
Author(s):  
Lawrence R DeChatelet ◽  
M Robert Cooper ◽  
Charles E McCall
Keyword(s):  
Amino Acids ◽  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Leukocyte Alkaline Phosphatase

Abstract Whereas the activity of leukocyte alkaline phosphatase is stimulated by Zn2+, it inhibits acid phosphatase activity. The degree of inhibition of acid phosphatase depends on the pH of the medium, being greater as the pH approaches neutrality. This inhibition may be at least partially reversed by the addition of amino acids, which suggests that interactions of Zn2+ and amino acids may play an important role in regulating the overall phosphatase activity of the leukocyte.

scholarly journals OBSERVATIONS ON THE ACID PHOSPHATASES OF EUGLENA GRACILIS

1965 ◽  
Vol 24 (2) ◽  
pp. 223-234 ◽  
Author(s):  
Jacob J. Blum
Keyword(s):  
Cell Division ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Actinomycin D ◽  
De Novo ◽  
Fluoride Concentration ◽  
Acid Phosphatases ◽  
De Novo Synthesis ◽  
Increased Activity

When a bleached strain of Euglena is maintained in a medium containing very low con centrations of phosphate, the acid phosphatase activity increases. The increase in acid phosphatase activity is prevented by Actinomycin D and by p-fluorophenylalanine (PFA), indicating that the increased activity is due to de novo synthesis of acid phosphatase. When phosphate is replenished, the acid phosphatase activity decreases to the level characteristic of uninduced cells before there is any appreciable cell division. When cell division resumes in the presence of PFA, the level of acid phosphatase activity remains approximately constant. This indicates that there are two different phosphatases: a constitutive enzyme, whose synthesis is insensitive to the presence of PFA, and an induced enzyme, whose synthesis is sensitive to PFA. These enzymes are not equally sensitive to changes in pH and in fluoride concentration, thus permitting them to be assayed individually in whole toluene-treated cells. Induced cells also acquire the ability to remove phosphate from the medium very rapidly.

Recessive Mutations in ACP4 Cause Amelogenesis Imperfecta

2021 ◽  
pp. 002203452110151
Author(s):  
Y.J. Kim ◽  
Y. Lee ◽  
Y. Kasimoglu ◽  
F. Seymen ◽  
J.P. Simmer ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
De Novo ◽  
Tooth Enamel ◽  
Activity Level ◽  
Amelogenesis Imperfecta ◽  
Catalytic Core ◽  
Enamel Thickness ◽  
Mutant Forms

Amelogenesis imperfecta (AI) is an innate disorder that affects the formation and mineralization of the tooth enamel. When diagnosed with AI, one’s teeth can be hypoplastic (thin enamel), hypomature (normal enamel thickness but discolored and softer than normal enamel), hypocalcified (normal enamel thickness but extremely weak), or mixed conditions of the above. Numerous studies have revealed the genes that are involved in causing AI. Recently, ACP4 (acid phosphatase 4) was newly found as a gene causing hypoplastic AI, and it was suggested that mutant forms of ACP4 might affect access to the catalytic core or the ability to form a homodimer. In this study, a Korean and a Turkish family with hypoplastic AI were recruited, and their exome sequences were analyzed. Biallelic mutations were revealed in ACP4: paternal (NM_033068: c.419C>T, p.(Pro140Leu)) and maternal (c.262C>A, p.(Arg88Ser)) mutations in family 1 and a paternal (c.713C>T, p.(Ser238Leu)) mutation and de novo (c.350A>G, p.(Gln117Arg)) mutation in the maternal allele in family 2. Mutations were analyzed by cloning, mutagenesis, immunofluorescence, immunoprecipitation, and acid phosphatase activity test. Comparison between the wild-type and mutant ACP4s showed a decreased amount of protein expression from the mutant forms, a decreased ability to form a homodimer, and a decreased acid phosphatase activity level. We believe that these findings will not only expand the mutational spectrum of ACP4 but also increase our understanding of the mechanism of ACP4 function during normal and pathologic amelogenesis.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).

Tartrate-resistant acid phosphatase activity and glutathione levels are modulated during hFOB 1.19 osteoblastic differentiation

2008 ◽  
Vol 39 (6) ◽  
pp. 627-634 ◽  
Author(s):  
Tatiana Salles de Souza Malaspina ◽  
Célio Xavier dos Santos ◽  
Ana Paula Campanelli ◽  
Francisco Rafael Martins Laurindo ◽  
Mari Cleide Sogayar ◽  
...  
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Osteoblastic Differentiation ◽  
Tartrate Resistant Acid Phosphatase
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