Acid phosphatase in Gaucher's disease.

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.

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.


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 ◽  
...  

1994 ◽  
Vol 106 (1) ◽  
pp. 223-232 ◽  
Author(s):  
K. S. Gellatly ◽  
GBG. Moorhead ◽  
SMG. Duff ◽  
D. D. Lefebvre ◽  
W. C. Plaxton

Pathology ◽  
1977 ◽  
Vol 9 (1) ◽  
pp. 85
Author(s):  
R.D. McEvoy ◽  
P.J. Phillips ◽  
R. Rowland ◽  
J.-B. Edwards ◽  
R. Bais

2014 ◽  
Vol 13 (1) ◽  
pp. 26-30
Author(s):  
Sonam Tashi Dolma ◽  
◽  
Davina Hijam ◽  
David Gangte ◽  
Ng. Arunkumar ◽  
...  

1965 ◽  
Vol 11 (11) ◽  
pp. 998-1008 ◽  
Author(s):  
Bernard Klein ◽  
Joseph Auerbach ◽  
Stanley Morgenstern

Abstract A procedure is presented for the automated determination of acid phosphatase activity in biological materials from either plant or animal origin. The Technicon N-7 flow diagram has been simplified, and the reagents for the measurement of enzymatically produced phenolic substances have been modified without loss of range or sensitivity. Both phenylphosphate and α-naphthylphosphate, introduced by Babson et al. (2, 3) for serum acid phosphatase, may be used as substrates. The Emerson reaction (alkaline aminoantipyrine and ferricyanide) with α-naphthol forms a more stable and reproducible color than the coupled product with tetrazotized o-dianisidine (Babson). Supporting data for these modifications are included.


1966 ◽  
Vol 12 (4) ◽  
pp. 226-233 ◽  
Author(s):  
Bernard Klein ◽  
Morris Oklander ◽  
Stanley Morgenstern

Abstract A procedure is presented for the automated determination of acid phosphatase activity in biological materials using the Robot Chemist. Although either phenylphosphate and α-naphthylphosphate may be used as substrate in this analysis, the procedure is described in detail for serum acid phosphatase using α-naphthylphosphate in 0.1 M citrate, pH 5.2, since this substrate is more selective for prostatic acid phosphatase in human serum. Enzymically generated aα- naphthol is determined by the Emerson reaction (alkaline aminoantipyrine and ferricyanide), modified for use with this automated system. Correlations are presented between the results obtained on the Robot Chemist and the identical procedure developed for the AutoAnalyzer.


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