Mechanisms of Phosphohydrolase Transport and of Homeostasis

Keiding, R.

doi:10.1111/j.1749-6632.1969.tb46417.x

Cited by 6 publications

(1 citation statement)

References 22 publications

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“…Our results using cellulose acetate electrophoresis show that in obstructive liver disease the main enzyme activity is found in the t2-globulin fraction with lesser activity in the atl-globulin fraction; the latter fraction is not found in normal control serum. These results are in agreement with previous results employing electrophoretic techniques relying mainlyonthe net charge on the protein molecule, and using, for example, paper ( Pellegrino, 1954), starch block (Rosenberg, 1959;Keiding, 1969), cellulose acetate (Korner, 1962), and agar gel (Wieme and Demeulenaere, 1971). Using polyacrylamide gel electrophoresis we found that in patients with obstructive liver disease the serum alkaline phosphatase showed a gross increase in the fast liver isoenzyme fraction with the appearance of several other isoenzyme fractions, the major contribution remaining at the origin.…”

Section: Discussionsupporting

confidence: 93%

The nature of the serum alkaline phosphatases in liver diseases

Price¹,

Sammons²

1974

J Clin Pathol

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The two main alkaline phosphatase isoenzymes in serum from patients with extrahepatic biliary obstruction have been purified. Properties of these isoenzymes, such as electrophoretic mobility, separation on gel filtration, ultracentrifugation characteristics, Michaelis constants, and sensitivity to neuraminidase have been studied and compared with the isoenzymes of liver and bile. The results show that there is an abnormal isoenzyme in the serum from these patients and that this isoenzyme is similar but not identical with the main bile isoenzyme. It is suggested that it may be associated with a lipoprotein carrier.

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