A comparative study of alkaline phosphatases among human placenta, bovine milk, hepatopancreases of shrimp Penaeus monodon (Crustacea: Decapoda) and clam Meretrix lusoria (Bivalvia: Veneidae): to obtain an alkaline phosphatase with improved characteristics as a reporter.
1. Alkaline phosphatases were purified from human placenta, bovine milk, shrimp and clam with a final spec. act. of 67,000, 32,000, 22,000 and 15,000 U/mg of protein respectively. 2. The alkaline phosphatase from Meretrix lusoria is unique with its thermostability at 65 degrees C for 30 min; whereas the remaining enzymes studied, including the human placental alkaline phosphatase, are inactivated and have negligible activities. 3. The alkaline phosphatase from Penaeus monodon can be differentiated by its pH optimum at 9.0; the remaining enzymes studied have their optimal pH at 10.0. 4. The alkaline phosphatases from shrimp and clam are proposed to be applied as "reporters" in the study of mammalian cells.
Chuang
N N
NN
Division of Biochemistry and Molecular Science, Academia Sinica, Nankang, Taipei, R. of China.
Yang
B C
BC
D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D049872:Bivalvia / Q000201:enzymology*; D004795:Enzyme Stability; D005260:Female; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008099:Liver / Q000201:enzymology; D008892:Milk / Q000201:enzymology*; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology; D033561:Penaeidae / Q000201:enzymology*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D000469:Alkaline Phosphatase