Biochemical Aspects of Blood Platelets (Peptidase, nucleotidase, acid and alkaline phosphatase activity in normal subjects, during menstruation and in some hemorrhagic disorders)

1954 ◽  
Vol 11 (5) ◽  
pp. 301-308 ◽  
Author(s):  
Emanuele Salvidio
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Blood Platelets ◽  
Normal Subjects ◽  
Acid And Alkaline Phosphatase ◽  
Hemorrhagic Disorders

scholarly journals Neutrophil alkaline phosphatase: comparison of enzymes from normal subjects and patients with polycythemia vera and chronic myelogenous leukemia

Blood ◽  
1975 ◽  
Vol 45 (3) ◽  
pp. 335-343
Author(s):  
D Rosenblum ◽  
SJ Petzold
Keyword(s):  
Alkaline Phosphatase ◽  
Polycythemia Vera ◽  
Phosphatase Activity ◽  
Chronic Myelogenous Leukemia ◽  
Alkaline Phosphatase Activity ◽  
Normal Subjects ◽  
Myelogenous Leukemia ◽  
Precipitin Line ◽  
Neutrophil Alkaline Phosphatase ◽  
Sepharose 4B

To determine whether decreased alkaline phosphatase activity in the granules from neutrophils of patients with chronic myelogenous leukemia (CML) was due to an absence of enzyme or the production of defective enzyme, we compared the immunologic properties of granule alkaline phosphatase derived from patients with CML with that of normal subjects and patients with polycythemia vera (PRV). Antisera prepared in rabbits against granule alkaline phosphatase purified from the neutrophils of a patient with PRV produced a single precipitin line of antigenic identity when reacted with extracts of normal, PRV, and CML neutrophil granules. A histochemical stain for alkaline phosphatase activity (alpha-naphthyl acid phosphate coupled with Fast Blue RR) specifically stained the precipitin line. A variety of quantitative precipitin techniques failed to produce satisfactory precipitation of alkaline phosphatase activity. Comparative analyses were therefore performed by affinity chromatography using goat antirabbit-gammaglobulin linked to Sepharose 4B to adsorb alkaline phosphatase complexed with rabbit gamma globulin. With this method, 100% of CML, normal, and PRV alkaline phosphatase could be adsorbed. Using limiting concentrations of antibody, a proportionally smaller fraction of enzyme activity was absorbed as the concentration of PRV alkaline phosphatase or normal alkaline phosphatase was increased. Extracts of CML granules containing comparable amounts of protein but 200-fold less alkaline phosphatase activity per milligram did not specifically reduce adsorption. Thus, in CML, we found no evidence that the granulocytes contained a large amount of antigenically normal but enzymatically defective alkaline phosphatase. Examination of electron micrographs revealed no significant differences in the number or distribution of granules in the granulocytes of normal subjects or patients with PRV or CML. This suggests that the low level of neutrophil alkaline phosphatase in CML granulocytes is the result of decreased enzyme content and not a consequence of synthesis of catalytically defective enzyme.

scholarly journals Neutrophil alkaline phosphatase: comparison of enzymes from normal subjects and patients with polycythemia vera and chronic myelogenous leukemia

Blood ◽  
1975 ◽  
Vol 45 (3) ◽  
pp. 335-343 ◽  
Author(s):  
D Rosenblum ◽  
SJ Petzold
Keyword(s):  
Alkaline Phosphatase ◽  
Polycythemia Vera ◽  
Phosphatase Activity ◽  
Chronic Myelogenous Leukemia ◽  
Alkaline Phosphatase Activity ◽  
Normal Subjects ◽  
Myelogenous Leukemia ◽  
Precipitin Line ◽  
Neutrophil Alkaline Phosphatase ◽  
Sepharose 4B

Abstract To determine whether decreased alkaline phosphatase activity in the granules from neutrophils of patients with chronic myelogenous leukemia (CML) was due to an absence of enzyme or the production of defective enzyme, we compared the immunologic properties of granule alkaline phosphatase derived from patients with CML with that of normal subjects and patients with polycythemia vera (PRV). Antisera prepared in rabbits against granule alkaline phosphatase purified from the neutrophils of a patient with PRV produced a single precipitin line of antigenic identity when reacted with extracts of normal, PRV, and CML neutrophil granules. A histochemical stain for alkaline phosphatase activity (alpha-naphthyl acid phosphate coupled with Fast Blue RR) specifically stained the precipitin line. A variety of quantitative precipitin techniques failed to produce satisfactory precipitation of alkaline phosphatase activity. Comparative analyses were therefore performed by affinity chromatography using goat antirabbit-gammaglobulin linked to Sepharose 4B to adsorb alkaline phosphatase complexed with rabbit gamma globulin. With this method, 100% of CML, normal, and PRV alkaline phosphatase could be adsorbed. Using limiting concentrations of antibody, a proportionally smaller fraction of enzyme activity was absorbed as the concentration of PRV alkaline phosphatase or normal alkaline phosphatase was increased. Extracts of CML granules containing comparable amounts of protein but 200-fold less alkaline phosphatase activity per milligram did not specifically reduce adsorption. Thus, in CML, we found no evidence that the granulocytes contained a large amount of antigenically normal but enzymatically defective alkaline phosphatase. Examination of electron micrographs revealed no significant differences in the number or distribution of granules in the granulocytes of normal subjects or patients with PRV or CML. This suggests that the low level of neutrophil alkaline phosphatase in CML granulocytes is the result of decreased enzyme content and not a consequence of synthesis of catalytically defective enzyme.

Monitoring of the inorganic polyphosphate accumulation and acid and alkaline phosphatase activity in Cunninghamella elegans strains using factorial design

2012 ◽  
Author(s):  
Luciana de Oliveira Franco ◽  
Thayza Christina Montenegro Stamford ◽  
Marcos Antônio Barbosa de Lima ◽  
Rita de Cassia Carvalho Maia ◽  
Tânia Lúcia Montenegro Stamford ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Factorial Design ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Cunninghamella Elegans ◽  
Inorganic Polyphosphate ◽  
Acid And Alkaline Phosphatase ◽  
Polyphosphate Accumulation
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