Structure and significance of N-linked sugar unit of human serum amyloid P component.

Human serum amyloid P component (SAP) was digested with pronase P and a glycopeptide fraction was obtained by gel-permeation chromatography. Carbohydrate and amino-acid composition of the glycopeptide suggested that each subunit of SAP possesses an N-linked glycan, but no O-linked ones. The N-linked oligosaccharide of SAP was obtained by hydrazynolysis. The structure of the oligosaccharide, which was deduced by sequential digestion with exoglycosidases and subsequent gel filtration, was identical or very similar to that of human transferrin. Removal of sialic acids from SAP reduced the calcium-dependent binding activity for agarose by 7%, suggesting the terminal sialic acids were partially responsible for the binding.