The analysis of alkaline phosphatase isoenzyme using 4-methylumbelliferyl phosphate as substrate on a cellulose acetate membrane

1979 ◽  
Vol 91 (3) ◽  
pp. 273-276 ◽  
Author(s):  
Fukuko Watanabe ◽  
Megumi Takano ◽  
Fumiko Tanaka ◽  
Nobuyuki Amino ◽  
Chozo Hayashi ◽  
...  
1977 ◽  
Vol 23 (1) ◽  
pp. 28-34 ◽  
Author(s):  
W H Siede ◽  
U B Seiffert

Abstract We present a new method for quantitative determination of alkaline phosphatase isoenzymes. This method consists of electrophoretic separation on cellulose acetate membranes, special fixation technique to avoid elution and diffusion of enzyme protein during incubation, specific staining, and quantitative evaluation by densitometric measurement. We highly recommend the precedure for routine clinical laboratory use. In all normal individuals we observe two isoenzymes of hepatic origin and one isoenzyme each of osseous, intestinal, and biliary origin. Quantitative normal values are presented. Precision of the method is calculated, the CV being less than 10%. The exactness of densitometric quantification is proved by comparison with kinetic assay of alkaline phosphatase isoenzymes by use of an elution method. Clinical implications of alkaline phosphatase isoenzymograms are reported and discussed in detail.


1985 ◽  
Vol 31 (7) ◽  
pp. 1198-1200 ◽  
Author(s):  
S B Rosalki ◽  
A Y Foo

Abstract Of 98 patients' specimens examined for alkaline phosphatase (EC 3.1.3.1) isoenzymes by electrophoresis on cellulose acetate membrane after incubation with neuraminidase, 50 showed only a single liver or bone isoenzyme staining band; in 15 of these, the tissue origin of the fraction could not be accurately identified from its electrophoretic location. In the remaining 48 specimens, both liver and bone fractions were identifiable, but in only 25 of these was the electrophoretic resolution sufficient to yield separate peaks on densitometry. In contrast, both liver and bone alkaline phosphatase isoenzymes were identified in 95 of the 98 specimens by affinity electrophoresis involving wheat-germ lectin, the detection of both fractions being in agreement with the results of sequential heat inactivation. The tissue origin of the enzyme bands was readily ascertainable from their consistent electrophoretic location in this medium, and in 89 of the specimens the isoenzyme fractions could be resolved into separate peaks on densitometry. We conclude that resolution of liver and bone alkaline phosphatase by incubation with neuraminidase followed by cellulose acetate electrophoresis is greatly inferior to that obtained by wheat-germ lectin affinity electrophoresis.


1990 ◽  
Vol 55 (12) ◽  
pp. 2933-2939 ◽  
Author(s):  
Hans-Hartmut Schwarz ◽  
Vlastimil Kůdela ◽  
Klaus Richau

Ultrafiltration cellulose acetate membrane can be transformed by annealing into reverse osmosis membranes (RO type). Annealing brings about changes in structural properties of the membranes, accompanied by changes in their permeability behaviour and electrical properties. Correlations between structure parameters and electrochemical properties are shown for the temperature range 20-90 °C. Relations have been derived which explain the role played by the dc electrical conductivity in the characterization of rejection ability of the membranes in the reverse osmosis, i.e. rRO = (1 + exp (A-B))-1, where exp A and exp B are statistically significant correlation functions of electrical conductivity and salt permeation, or of electrical conductivity and water flux through the membrane, respectively.


Chemosphere ◽  
2015 ◽  
Vol 136 ◽  
pp. 204-210 ◽  
Author(s):  
Hyeon-gyu Choi ◽  
Moon Son ◽  
SangHyeon Yoon ◽  
Evrim Celik ◽  
Seoktae Kang ◽  
...  

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