Lisowska E, Waśniowska K
Eur J Biochem. 1978 Jul 17;88(1):247-52. doi: 10.1111/j.1432-1033.1978.tb12444.x.
The major glycopeptides purified from the tryptic digests of M and N blood-group glycoproteins were degraded with cyanogen bromide into two fragments. The chemical composition and serological activities of the fragments obtained were determined. The results show that M and N blood-group determinants are located on the smaller N-terminal fragments, containing 8 amino acid residues and only alkali-labile oligosaccharide chains. Two of 8 amino acid residues are different in M-specific and N-specific glycopeptide. All glycopeptides obtained inhibited Vicia graminea anti-N lectin, but the N-terminal fragment of N-glycopeptide was a better inhibitor than others. Treatment with neuraminidase or acetylation of amino groups destroyed the M and N blood-group activity and increased the activity towards Vicia graminea anti-N lectin of all glycopeptides studied.
从M和N血型糖蛋白的胰蛋白酶消化物中纯化得到的主要糖肽，用溴化氰降解为两个片段。测定了所得片段的化学组成和血清学活性。结果表明，M和N血型决定簇位于较小的N端片段上，该片段含有8个氨基酸残基且只有对碱不稳定的寡糖链。在M特异性和N特异性糖肽中，8个氨基酸残基中有两个不同。所有得到的糖肽都能抑制蚕豆抗N凝集素，但N-糖肽的N端片段是比其他片段更好的抑制剂。用神经氨酸酶处理或对氨基进行乙酰化会破坏M和N血型活性，并增加所研究的所有糖肽对蚕豆抗N凝集素的活性。
