A novel lectin isolated from the hemolymph of the marine hair crab Erimacrus isenbeckii.
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.
Na
Young Jun
YJ
Physical Pharmacy Laboratory, College of Pharmacy, Chung-Ang University, 221 Huksuk-Dong, Dongjak-Ku, Seoul, Korea.
Kim
Yu Jeong
YJ
Park
Byung Tae
BT
Jung
Byung Wook
BW
Hwang
Kwang Woo
KW
Kim
HaHyung
H
D000595:Amino Acid Sequence; D000818:Animals; D003386:Brachyura; D004591:Electrophoresis, Polyacrylamide Gel; D006384:Hemagglutination / Q000187:drug effects; D006458:Hemolymph / Q000737:chemistry*; D037102:Lectins / Q000302:isolation & purification*; D008358:Mannose / Q000494:pharmacology; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012260:Ribonucleases / Q000037:antagonists & inhibitors
D037102:Lectins; D012260:Ribonucleases; C029600:ribonuclease B; D008358:Mannose