A novel lectin isolated from the hemolymph of the marine hair crab Erimacrus isenbeckii
- Authors
- Na, Young Jun; Kim, Yu Jeong; Park, Byung Tae; Jung, Byung Wook; Hwang, Kwang Woo; Kim, HaHyung
- Issue Date
- Aug-2007
- Publisher
- BENTHAM SCIENCE PUBL LTD
- Keywords
- erimacrus isenbeckii; crab; hemolymph; lectin; O-acetylsialic acid; mannose
- Citation
- PROTEIN AND PEPTIDE LETTERS, v.14, no.8, pp 800 - 803
- Pages
- 4
- Journal Title
- PROTEIN AND PEPTIDE LETTERS
- Volume
- 14
- Number
- 8
- Start Page
- 800
- End Page
- 803
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24204
- DOI
- 10.2174/092986607781483714
- ISSN
- 0929-8665
1875-5305
- 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 anion-exchange 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 degrees 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.
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Collections - College of Pharmacy > School of Pharmacy > 1. Journal Articles
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