Evidence of the Presence of Two distinct Alkaline Phosphatases in Serratia Marcescens

PDF

Authors
  1. Bhatti, A.R.
  2. Alvi, A.Z.
  3. Chaudhry, G.R.
Corporate Authors
Defence Research Establishment Suffield, Ralston ALTA (CAN)
Abstract
Certain strains of Serratia marcescens synthesized two different types of alkaline phosphatase (APase), constitutive (CAPase) and inducible (IAPase) APases, in low phosphate medium. Synthesis of the IAPase was repressed in the presence of high phosphate. Purification and separation of these electrophoretically distinct APases was achieved by using fractional (NH4)2SO4 precipitation, adsorption on a DEAE-cellulose column and elution of enzymes by a linear sodium chloride gradient. Starch gel electrophoresis of certain fractions revealed the separation of not only IAPase from CAPase but its separation into four distinct isozymes. CAPase gave maximum enzyme activity around pH 9.5, whereas for IAPase a broad range of enzyme activity was found between pH 8.5 and 10.5. Reversible inactivation at low pH occured for IAPase but very little with CAPase was more thermolabile than IAPase at 95C. The two APases were found to be distinct in their kinetic as well as immunological properties, suggesting two distinct enzyme species.
Report Number
DRES-OL-98-008 — Reprint
Date of publication
01 Feb 2000
Number of Pages
8
Reprinted from
FEMS Microbiology Letters, Vol 182, 2000, p 131-135
DSTKIM No
CA000544
CANDIS No
512708
Format(s):
Hardcopy;Document Image stored on Optical Disk

Permanent link

Document 1 of 1

Date modified: