Chitovibrin: a chitin-binding lectin fromVibrio parahemolyticus |
| |
| Authors: | Otto S. Gildemeister Betty C. R. Zhu Roger A. Laine |
| |
| Affiliation: | (1) Department of Biochemistry, Department of Chemistry, Louisiana State University and The Louisiana Agricultural Center, 70803 Baton Rouge, LA, USA;(2) Present address: Medical Center, Digestive Disease and Nutrition, University of Massachusetts, 01655 Worcester, MA |
| |
| 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.Abbreviations (GlcNAc)2 N,N -diacetylchitobiose - SDS-PAGE sodium dodecyl sulphate-polyacrylamide gel electrophoresis - PTS phosphotransferase system |
| |
| Keywords: | chitin-binding lectin ![]("</a) /content/h10613370l246576/xxlarge8216.gif" alt=" lsquo" align=" BASELINE" BORDER=" 0" >chitovibrin /content/h10613370l246576/xxlarge8217.gif" alt=" rsquo" align=" BASELINE" BORDER=" 0" > Vibrio parahemolyticus |
| 本文献已被 SpringerLink 等数据库收录！ |
|
