ACL-I, a lectin from the marine sponge Axinella corrugata: isolation, characterization and chemotactic activity

Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP
Roger R DreschMagdolna M Vozári-Hampe

Abstract

The lectin from the marine sponge Axinella corrugata (ACL-I) was purified by affinity chromatography on rabbit erythrocytic stroma incorporated into a polyacrylamide gel followed by gel filtration on Ultrogel AcA 44 column. Purified ACL-I is a hexameric glycoprotein with a Mr of 82.3 kDa estimated by SDS-PAGE and 78.5 kDa by FPLC on Superose 12 HR column. The pI of lectin is 6.3 and ACL-I is constituted of 13.9 kDa similar subunits some of them linked by disulphide bridges. This lectin agglutinates native rabbit, goat and dog erythrocytes and in less extent human erythrocytes. The hemagglutinating activity is independent of Ca(2+), Mg(2+) and Mn(2+), but it is strongly inhibited by carbohydrates containing N-acetyl groups. ACL-I is stable up to 70 degrees C for 30 min, with optimum pH between 7 and 8, and it is also resistant to enzymatic proteolysis in vitro. In the presence of reducing or denaturant agents, the lectin activity decreases. ACL-I displays chemotactic effect on rat neutrophil in vitro which is inhibited by N-acetyl-d-glucosamine.

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Oct 23, 2013·The International Journal of Biochemistry & Cell Biology·Rômulo Farias CarneiroAlexandre Holanda Sampaio
Aug 12, 2015·Marine Drugs·Johan GardèresWerner E G Müller
Jan 23, 2016·International Journal of Biological Macromolecules·Shuai LiuWei Li
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Jan 3, 2013·Journal of Molecular Recognition : JMR·Rômulo Farias CarneiroAlexandre Holanda Sampaio
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