Abstract
Almond glycopeptidase cleaves specifically fl-aspartyl-glucosylamine linkages in glycoproteins with asialocarbohydrate moieties [1-3]. We have reported that the enzyme is an excellent tool in biochemical analyses of asparagine-linked oligosaccharides such as a xylose-containing oligosaccharide of stem bromelain [4], high-mannose-type and hybrid-type oligosaccharides in hen ovalbumin [5] and a complex-type oligosaccharide in human fibrinogen [6]. Neuraminidase is the only enzyme that has been available for the characterization of glycoproteins in correlated biochemical and histochemical systems. Methods for the histochemical demonstration of glycoproteins have not yet led to the differentiation of serum-type (Nglycosidically linked) and mucin-type (O-glycosidically linked) carbohydrates, which have precisely been defined in biochemical terms. We have attempted to employ the glycopeptidase in biochemical and histochemical analyses of glycoproteins in human placenta and umbilical cord tissues. Biochemically, glycoproteins with asparagine-linked oligosaccharides of complex type were shown to be present commonly in different components of the tissues. Histochemically, digestion with the enzyme reduced apparently the staining for neutral carbohydrates in particular histo-
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