Abstract
Hemagglutinin activity toward mammalian erythrocytes was detected in the hemolymph of the sea prawn Parapenaeus longirostris. Two lectins and one agglutinin were isolated from the hemolymph of this animal after adsorption on formalinized rabbit erythrocytes. The native and the subunit molecular mass estimated with gradient nondenaturing-PAGE and SDS-PAGE was 440 kDa (27-kDa subunit) for one of the lectins, 210 kDa (36-kDa subunit) for the other, and 160 kDa (16- and 18-kDa subunit) for the agglutinin. Both lectins recognized N -acylaminosugars but the 440-kDa lectin was specific for N -acetylneuraminic acid and the 210-kDa lectin for N -acetylgalactosamine. Hemagglutination by P. longirostris lectins and agglutinin required divalent cations, while after EDTA treatment the 440-kDa (27kDa subunit) lectin dissociated to 60-kDa oligomers. Both lectins and the agglutinin strongly agglutinated formalinized Pseudomonas aeruginosa and Escherichia coli bacteria and may contribute to the defense against specific microorganisms.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
