Antibodies to porcine uteroferrin used in measurement of human tartrate-resistant acid phosphatase.

1987 ◽  
Vol 33 (10) ◽  
pp. 1832-1836 ◽  
Author(s):  
Z O Echetebu ◽  
T M Cox ◽  
D W Moss

Abstract The immunological similarity between human tartrate-resistant acid phosphatase (EC 3.1.3.2) and porcine uteroferrin previously reported for the isoenzyme from spleens of patients with leukemic reticuloendotheliosis (Ketcham et al., J Biol Chem 1985;260:5768-76) has been confirmed for partly purified acid phosphatase found in the spleen of a patient with Gaucher's disease, and for the corresponding isoenzyme in other tissues and serum. Anti-uteroferrin antibodies raised in rabbits have been used to demonstrate the feasibility of their application in an immunoassay for tartrate-resistant acid phosphatase in serum.

The Lancet ◽  
1968 ◽  
Vol 292 (7563) ◽  
pp. 358-359 ◽  
Author(s):  
G.P. Perona ◽  
C. Baccichetti ◽  
R. Tenconi

1980 ◽  
Vol 26 (3) ◽  
pp. 371-382
Author(s):  
D B Robinson ◽  
R H Glew

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.


1974 ◽  
Vol 32 (02/03) ◽  
pp. 665-669 ◽  
Author(s):  
S Yatziv ◽  
M White ◽  
A Eldor

SummaryFive platelet lysosomal enzyme activities were estimated in 22 normal individuals and in 5 patients with Gaucher’s disease: ß-D-galactosidase, N-Acetyl-ß-D-glucosa-minidase, N-Acetyl-ß-D-galactosaminidase acid-phosphatase, and ß-D-glucuronidase.In the 5 patients with Gaucher’s disease the specific activities for the first four of these enzymes were significantly higher than in normal individuals. The activity of acid-phosphatase, on the other hand, was lower in G. d. than in normals. The release of the 5 lysosomal enzymes from platelets upon incubation with thrombin was also examined in the same two groups. The only lysosomal enzyme that was not released from normal platelets was acid-phosphatase. In Gaucher’s patients, on the other hand, acid-phosphatase was invariably released from platelets when incubated with thrombin. The release of the other four enzymes from platelets of Gaucher patients was similar to that of normal controls.


Metabolism ◽  
1978 ◽  
Vol 27 (7) ◽  
pp. 801-814 ◽  
Author(s):  
James P. Chambers ◽  
Stephen P. Peters ◽  
Robert H. Glew ◽  
Robert E. Lee ◽  
Leo R. McCafferty ◽  
...  

1980 ◽  
Vol 26 (3) ◽  
pp. 371-382 ◽  
Author(s):  
D B Robinson ◽  
R H Glew

Abstract Increased acid phosphatase activity in the serum and tissues of patients with Gaucher's disease has now been recognized for two decades, but as yet no relation has been established between the enzyme and the etiology and progress of the disease. Here, we review results obtained by various investigators, ranging from a consideration of the methods used for the evaluation of serum acid phosphatase in Gaucher's disease to the most recent findings regarding the purification and characterization of two acid phosphatase isoenzymes from the spleen from patients with Gaucher's disease. We also discuss the intracellular location of tissue acid phosphatase in patients with Gaucher's disease and its contribution to the increased activity in serum.


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