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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

A Novel Lectin Isolated from the Hemolymph of the Marine Hair Crab Erimacrus isenbeckii

Author(s): Young Jun Na, Yu Jeong Kim, Byung Tae Park, Byung Wook Jung, Kwang Woo Hwang and HaHyung Kim

Volume 14, Issue 8, 2007

Page: [800 - 803] Pages: 4

DOI: 10.2174/092986607781483714

Price: $65

Abstract

A lectin that induces hemagglutination activity in mouse and rabbit erythrocytes has been purified from the hemolymph of the marine hair crab Erimacrus isenbeckii. The results of SDS-PAGE, gel-filtration, affinity and anionexchange chromatography indicate that this lectin, designated EIL (E. isenbeckii lectin), was successfully purified as a single protein, and comprises a mixture of a major (90%) dimeric and a minor (10%) oligomeric protein with a molecular mass of 116 kDa, with covalent linking between two subunits of 62 and 54 kDa. The activity was maximal at pH 5.6 – 8.0 and at temperatures below 50°C. The N-terminal amino acid sequences were determined, and these differed greatly from those of other reported lectins from invertebrates, vertebrates, or plants. EIL binds with high specificities to both the O-acetylsialic acid and mannose that are present in bacterial pathogens, which suggests that EIL can act as a defense protein against infection in this crab.

Keywords: Erimacrus isenbeckii, crab, hemolymph, lectin, O-acetylsialic acid, mannose


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