Chitovibrin: a chitin-binding lectin from Vibrio parahemolyticus
A novel 134 kDa, calcium-independent chitin-binding lectin, 'chitovibrin', is secreted by the marine bacterium Vibrio parahemolyticus, inducible with chitin or chitin-oligomers. Chitovibrin shows no apparent enzymatic activity but exhibits a strong affinity for chitin and chito-oligomers >dp9. The protein has an isoelectric pH of 3.6, shows thermal tolerance, binds chitin with an optimum at pH 6 and is active in 0-4 m NaCl. Chitovibrin appears to be completely different from other reported Vibrio lectins and may function to bind V. parahemolyticus to chitin substrates, or to capture or sequester chito-oligomers. It may be a member of a large group of recently described proteins in Vibrios related to a complex chitinoclastic (chitinivorous) system. © 1994 Chapman & Hall.
Publication Source (Journal or Book title)
Gildemeister, O., Zhu, B., & Laine, R. (1994). Chitovibrin: a chitin-binding lectin from Vibrio parahemolyticus. Glycoconjugate Journal, 11 (6), 518-526. https://doi.org/10.1007/BF00731302