Spontaneous conversion of carp liver AcPase I and some properties of its asialo-form.
Evidence is given for a spontaneous conversion of AcPase I to a more basic form due to autolytic loss of sialic acid. To investigate whether the presence of sialic acid in the enzyme molecule is of any physiological significance some physico-chemical properties of an enzymatically obtained asialo-AcPase I were studied. It has been shown that the asialo-form retained the properties of the native enzyme in respect to thermostability and pH-stability but modified slightly the hydrolytic activities of some phosphorylated compounds, and this might be of significance under physiological conditions.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002347:Carps / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D003530:Cyprinidae / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology*; D019158:N-Acetylneuraminic Acid; D012794:Sialic Acids / Q000378:metabolism; D013696:Temperature
D012794:Sialic Acids; D000135:Acid Phosphatase; D019158:N-Acetylneuraminic Acid