Studies on the oligosaccharide heterogeneity of the isoelectric forms of the lower molecular weight acid phosphatase of frog liver.
1. The lower molecular weight, heterogeneous acid phosphatase (AcPase) from the frog liver (Rana esculenta) containing AcPase I, II, III and IV was separated into enzymatically active components by isoelectric focusing in an immobilized pH gradient. 2. The blotted enzyme bands were characterized by their different binding patterns obtained with the lectins concanavalin A, wheat germ agglutinin (WGA), Lens culinaris hemagglutinin (LcH) and peanut agglutinin (PNA). 3. In situ neuraminidase treatment reduced the staining intensity of some WGA-bands and increased that of PNA-bands. 4. The finding that AcPases I, II, III and IV differ in their carbohydrate chain composition, together with previous results showing different bioactivities of AcPases III and IV, indicates a correlation between the glycosylation state of enzyme forms and their physiological action.
Kubicz
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Institute of Biochemistry, University of Wroclaw, Poland.
Szalewicz
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Chrambach
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D000135:Acid Phosphatase / Q000737:chemistry / Q000302:isolation & purification*; D000818:Animals; D006031:Glycosylation; D007525:Isoelectric Focusing; D037102:Lectins; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009439:Neuraminidase; D009844:Oligosaccharides / Q000302:isolation & purification*; D011893:Rana esculenta
D037102:Lectins; D009844:Oligosaccharides; D000135:Acid Phosphatase; D009439:Neuraminidase