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Purification and Characterization of a Soluble Peroxidase of Rat Preputial Gland: Comparison with Lactoperoxidase

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Title Purification and Characterization of a Soluble Peroxidase of Rat Preputial Gland: Comparison with Lactoperoxidase
 
Creator De, Prabir K
Banerjee, Ranajit K
 
Subject Cell Biology & Physiology
 
Description A highly active ,soluble peroxidase (donor: H202 oxidoreductasc EC I.i !.i.7) has bccn purified from the preputial gland of the
rat by hydroxylapatitc chromatography, ammonium sulfate fraclionation, Sephadex gel filtration and affinity chromatography on
con A-Sepharosc. The enzyme shows apparent homogcneity when analysed by acid and alkaline-PAGE. Its molecular, spectral,
kinetic and catalytic properties were compared with those of bovine lactoperoxidase (LPO). Preputial gland pcroxidase (PPO) is
a glycoprotein of molecular weight of 711-73 kDa slightly lower (78 kDa) than that of LPO. Using isoelectric focussing, PPO was
resolved into eight different closely spaced protein species spanning a pl range of 5.4 to 6.4, while LPO focusscs into several
closely spaced protein bands in the pl range 8.5-9.3. PPO is similar to LPO in its spectral (Soret) and some kinetic properties,
but it differs significantly from LPO in substrate (H,_O2) tolerance and substrate inactivation. PPO also differs from LPO in
showing differential inactivation by SDS. Both enzymes arc glycoproteins and although concanavalin A (con A) showed a
variable interaction with both enzymes, wheat germ agglutinin interacted specifically with LPO only. We suggest that PPO, the
~cretory peroxidase of the preputial gland, differs significantly from LPO in its molecular and catalytic properties
 
Publisher Elsevier
 
Date 1992
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1787/1/BIOCHIMICA_ET_BIOPHYSICA_ACTA___1120(_2)167%2D172;1992[38].pdf
De, Prabir K and Banerjee, Ranajit K (1992) Purification and Characterization of a Soluble Peroxidase of Rat Preputial Gland: Comparison with Lactoperoxidase. BBA - Biochimica et Biophysica Acta, 1120 (2). pp. 167-172.
 
Relation http://dx.doi.org/10.1016/0167-4838(92)90265-F
http://www.eprints.iicb.res.in/1787/