Stelmach H, Jaroszewicz L
Zakładu Chemii Fizycznej, Instytutu Chemii AM w Białymstoku.
Rocz Akad Med Bialymst (1989). 1988;33-34:23-32.
Pig thyroid myoinositol-phosphate synthase was purified about 30 times using ammonium sulphate fractionation and DEAE cellulose chromatography. The enzyme preparation showed the activity of more than 70 mU/mg of protein. A partially purified synthase is a very labile enzyme. Its activity showed optimum value at pH 7.0. This activity appeared to be controlled by NH4+, Na+, and Li+ ions. The biological role of thyroid synthase has been discussed.
