scholarly journals Effect of zinc in the glycine electrode buffer on detection of alkaline phosphatase activity after polyacrylamide gel electrophoresis.

2000 ◽  
Vol 44 (1) ◽  
pp. 15-19
Author(s):  
Shuichi Hashimoto ◽  
Toshiyuki Toen
1981 ◽  
Vol 11 (2) ◽  
pp. 201-206
Author(s):  
Jack R. Sutherland ◽  
Ute Rink ◽  
E. E. McMullan ◽  
T. A. D. Woods

Extracts of samples from Caloscyphafulgens infested and noninfested Sitka spruce (Piceasitchensis (Bong.) Carr.) seed lots and diseased and healthy seeds were separated by electrophoresis on polyacrylamide gels and stained for esterase (EC 3.1.1.1), leucine aminopeptidase (EC 3.4.1.1), acid phosphatase (EC 3.1.3.2), alkaline phosphatase (EC 3.1.3.1), glucose-6-phosphatase (EC 3.1.3.9), malate dehydrogenase (EC 1.1.1.37), isocitrate dehydrogenase (EC 1.1.1.42), 6-phosphogluconate dehydrogenase (EC 1.1.1.43) and alcohol dehydrogenase (EC 1.1.1.1). Several differences were detected between the isozyme patterns of disease-free and infested samples, but the main difference was the latter's high alkaline phosphatase activity. By using gel electrophoresis, (i) a qualitative analysis was developed, based on the presence or absence of alkaline phosphatase, to distinguish infested from disease-free seed lots, and (ii) the high alkaline phosphatase activity of infested samples was determined to be of pathogenic origin. By determining the alkaline phosphatase activity of samples with known numbers of diseased seeds, a prediction equation was derived relating enzyme activity and disease incidence. Correlation analyses showed significant (P = 0.01) correlations between disease incidence estimates obtained by this technique and plating of surface-sterilized seeds on water agar.


Author(s):  
TJ Brooks ◽  
HG Sammons

Loss of activity of the isoenzymes of γ-glutamyl transferase and alkaline phosphatase has been shown to occur during electrophoresis on polyacrylamide gel. After studying the possible factors concerned in this loss, reasonable recovery from the gel can be obtained only for the isoenzyme staying at the origin. Maximum recovery is 60% for origin γ-glutamyl transferase and 92% for origin alkaline phosphatase.


Development ◽  
1971 ◽  
Vol 26 (3) ◽  
pp. 339-349
Author(s):  
Sallie B. Freeman

A study was made of the emergence of certain enzymes during the embryogenesis of Ilyanassa. Lobeless and normal embryos were compared in order to determine the effect of polar lobe removal on subsequent molecular developments. Polyacrylamide gel electrophoresis in capillary tubes, a technique requiring only small numbers of embryos, was used to obtain the isozyme patterns of alkaline phosphatases and of esterases. It was found that lobe removal interfered with the emergence of normal isozyme patterns of alkaline phosphatase and esterase during development. Certain bands of enzyme activity were severely reduced or absent while others appeared to be normal. The results provide further evidence that the influence of the polar lobe on development is of a specific nature.


1981 ◽  
Vol 198 (1) ◽  
pp. 9-15 ◽  
Author(s):  
G R Rao ◽  
H N Aithal ◽  
F G Toback ◽  
G S Getz

Lysosome formation was induced in cells of the renal medulla by feeding rats on a K+-deficient diet. The role of the endoplasmic reticulum in the production of acid phosphatase, a typical lysosomal enzyme, was examined. Lysosomal and microsomal fractions were prepared for study by differential centrifugation of homogenates of renal papilla and inner stripe of red medulla. Acid phosphatase activity in the microsomal fraction was distinguished from the activity in the lysosomal fraction in normal tissue by differences in pH optima, tartrate inhibition, distribution of multiple forms after polyacrylamide-gel electrophoresis and detergent-sensitivity. During progressive K+ depletion, acid phosphatase activity in both microsomal and lysosomal fractions of the tissue increased 3-fold. In the lysosomes, K+ depletion was associated with the appearance of a new band of acid phosphatase. The neuraminidase-sensitivity of this band on polyacrylamide-gel electrophoresis indicated that the enzyme protein had been modified by the addition of sialic acid residues. K+ depletion also altered the lysosomal enzyme so that thiol compounds were able to stimulate its activity.


1973 ◽  
Vol 17 (2) ◽  
pp. 71-76
Author(s):  
Manabu Masuzawa ◽  
Takenobu Kamata ◽  
Yasuhiko Sakoyama ◽  
Yasuto Chiba ◽  
Zen-ichi Ogita

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