, Volume 48, Issue 5, pp 498–500 | Cite as

An agglutinin with unique specificity for N-glycolyl sialic acid residues of thyroglobulin in the hemolymph of a marine crabScylla serrata (Forskal)

  • P. D. Sr. Mercy
  • M. H. Ravindranath
Research Articles


A novel agglutinin with specificity for sialic acid sequence of sugars in thyroglobulin is identified in the hemolymph ofScylla serrata. The physico-chemical characteristics of its binding affinity, such as pH and temperature optima, and cationic requirements are defined. N-glycolyl neuraminic acid (NeuGc) (at 0.6 mM), in contrast to N-acetyl neuraminic acid (NeuAc) (at >5.0 mM), is the potent inhibitor of hemagglutination. Bovine and porcine thyroglobulins containing NeuGc, inhibited the agglutination. NeuGc-acid glycoprotein fraction (bovine) but not NeuAc-acid glycoprotein fraction (human) inhibited the hemagglutination. The inability of other NeuGc-glycoproteins (bovine submaxillary mucin) to inhibit the agglutination suggests that the agglutinin may also recognize glycosidic linkage associated with NeuGc. The potential of the agglutinin in identifying NeuGc containing human tumor associated antigens is discussed.

Key words

Hemolymph agglutinin sialic acids N-acetyl neuraminic acid (NeuAc) N-glycolyl neuraminic acid (NeuGc) thyroglobulin glycosidic linkages 


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Copyright information

© Birkhäuser Verlag Basel 1992

Authors and Affiliations

  • P. D. Sr. Mercy
    • 1
  • M. H. Ravindranath
    • 2
  1. 1.Department of ZoologyHoly Cross CollegeTamilnadu(India)
  2. 2.Division of Oncology, Department of SurgeryUniversity of CaliforniaLos AngelesUSA

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