ISSN:
1573-4986
Keywords:
chitin-binding lectin
;
‘chitovibrin’
;
Vibrio parahemolyticus
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract A novel 134 kDa, calcium-independent chitin-binding lectin, ‘chitovibrin’, is secreted by the marine bacteriumVibrio 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 0–4m NaCl. Chitovibrin appears to be completely different from other reported Vibrio lectins and may function to bindV. 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00731302
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