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The amino‐terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins
Author(s) -
Petersen Torben E.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80700-2
Subject(s) - biochemistry , protein superfamily , amino acid , chemistry , thrombomodulin , peptide sequence , asialoglycoprotein receptor , amino terminal , disulfide bond , microbiology and biotechnology , biology , thrombin , gene , immunology , in vitro , platelet , hepatocyte
Amino acid sequence alignment of the amino‐terminal domain of thrombomodulin and pancreatic stone protein with the hepatic asialoglycoprotein receptor shows that these proteins are homologous. From the known disulfide bridge pattern of other proteins belonging to the same family two disulfide bonds can be predicted. The homology raises the question whether the amino‐terminal part of thrombomodulin and the pancreatic protein binds carbohydrate or perhaps like tetranectin have a specific affinity for other proteins.