Phospholipid analysis and fractional reconstitution of the ice nucleation protein activity purified from Escherichia coli overexpressing the inaZ gene of Pseudomonas syringae (Journal article)

Palaiomylitou, M. A./ Kalimanis, A./ Koukkou, A. I./ Drainas, C./ Anastassopoulos, E./ Panopoulos, N. J./ Ekateriniadou, L. V./ Kyriakidis, D. A.

Ice nucleation protein was partially purified from the membrane fraction of E. coli carrying inaZ from Pseudomonas syringae. The ice nucleation protein was totally localized in the bacterial envelope and was extracted by either salt (0.25 M NH4Cl) or the nonionic detergent Tween 20. The extracted protein was partially purified by sequential passage through DEAE-52 cellulose and Sephacryl-S400 columns. The activity of the purified protein was lost after treatment with phospholipase C, and its activity was subsequently restored by addition of the naturally occurring Lipid phosphatidylethanolamine. These results suggest that ice nucleation proteins have a requirement for lipids that reconstitute a physiological hydrophobic environment similar to the one existing in vivo, to attain and maintain a structure that enables ice catalysis. (C) 1998 Academic Press.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: ice nucleation protein,inaz gene,e-coli,reconstitution,expression,identification,purification,mutagenesis,product,invitro,nuclei,lipids
ISSN: 0011-2240
Link: <Go to ISI>://000075366600008
Publisher: Elsevier
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

Files in This Item:
File Description SizeFormat 
Palaiomylitou-1998-Phospholipid analysi.pdf163.46 kBAdobe PDFView/Open    Request a copy

 Please use this identifier to cite or link to this item:
  This item is a favorite for 0 people.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.