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Phospholipase C from two bacterial strains acts differently on pure phospholipids and membrane bound glycosylphosphatidylinositol (GPI) anchors

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Title Phospholipase C from two bacterial strains acts differently on pure phospholipids and membrane bound glycosylphosphatidylinositol (GPI) anchors
 
Creator Rastogi, Arshi
Hutchinson, Tarun E
Pereira, Ben M J
 
Subject Phospholipase C
Bacillus cereus
Bacillus thuringiensis
Phospholipids
Microsomal membrane
Sperm plasma membrane
Glycosylphosphatidylinositol (GPI) anchor
Alkaline phosphatase
ATPase
Inhibitors
 
Description 92-99
Phospholipase C (PLC) was purified to homogeneity
from the culture filtrate of Bacillus cereus (65-fold, 540 U/mg protein)
and B. thuringiensis (76-fold, 306 U/mg protein) by conventional
techniques of enzyme purification. The purified

enzymes have the molecular mass of 34 kDa and 38 kDa
respectively, as determined by SDS-PAGE. Both the PLCs exhibited identical
sensitivity to pH,
temperature, cations, anions and
inhibitors like glutathione and p-chloromercuribenzoate. PLC-Bc showed a
preference for phosphatidylinositol, while PLC-Bt favoured phosphatidylcholine
as the substrate. Although both the enzymes were able to hydrolyze pure
phosphatidylinositol, distinct differences were observed in their activity on
phosphatidylinositol-anchored membrane proteins. PLC-Bc cleaved and

released alkaline phosphatase, a GPI-anchored
marker enzyme from microsomal membranes to a greater extent, than PLC-Bt. Experiments
with sperm membranes, followed by SOS-PAGE revealed that the pattern of
proteins released from their

GPI-anchors by PLC-Bc and PLC-Bt were dissimilar.
Although some proteins were cleaved in common by both PLCs, some others
including a prominent 57 kDa protein were resistant to PLC-Bt, but sensitive to
cleavage by PLC-Bc. The type

of modification in the GPI anchor, special
environment on membranes, and relative charge of host plasma membrane to the charge
of PLC may be the factors that are responsible for the differential action of
two enzymes.
 
Date 2015-01-16T11:35:43Z
2015-01-16T11:35:43Z
2005-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/30381
 
Language en_US
 
Relation C 12 Q 1/100
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.42(2) [April 2005]