Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens

Kshama Kumari, Naseem Ansari, Manju Saxena, Yogesh C. Awasthi, Satish Srivastava

Research output: Contribution to journal › Article

2 Citations (Scopus)

Abstract

Dinitrophenyl S-glutathione (Dnp-SG) ATPase which catalyses the hydrolysis of ATP in the presence of GSH-conjugates has been implicated previously in the transport of these conjugates. In the present studies we demonstrate that Dnp-SG ATPase is present in bovine lens epithelium and cortex. The specific activity per mg membrane protein was found to be 75-fold higher in the epithelium as compared to the cortex. No enzyme was detected in the nuclear region of the lens. Dnp-SG ATPase was purified from bovine lens epithelium and cortex using Dnp-SG-Sepharose 6MB affinity chromatography. The partially purified Dnp-SG ATPase had two distinct Km values, 120 μM and 1·0 mM. The antibodies raised against human erythrocyte Dnp-SG ATPase cross-reacted with the bovine lens epithelium Dnp-SG ATPase which was identified by Western blot as a band corresponding to an approximate Mr value of 80000 Da.

Original languageEnglish (US)
Pages (from-to)243-247
Number of pages5
JournalExperimental Eye Research
Volume57
Issue number2
DOIs
StatePublished - Aug 1993

Fingerprint

Lenses
Adenosine Triphosphatases
Epithelium
Affinity Chromatography
Glutathione
S-(dinitrophenyl)glutathione ATPase
Membrane Proteins
Hydrolysis
Adenosine Triphosphate
Erythrocytes
Western Blotting
Antibodies
Enzymes

Keywords

  • bovine lens
  • Dnp-SG ATPase
  • glutathione
  • glutathione conjugates
  • xenobiotic transport

ASJC Scopus subject areas

  • Sensory Systems
  • Ophthalmology

Cite this

Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens. / Kumari, Kshama; Ansari, Naseem; Saxena, Manju; Awasthi, Yogesh C.; Srivastava, Satish.

In: Experimental Eye Research, Vol. 57, No. 2, 08.1993, p. 243-247.

Research output: Contribution to journal › Article

Kumari, K, Ansari, N, Saxena, M, Awasthi, YC & Srivastava, S 1993, 'Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens', Experimental Eye Research, vol. 57, no. 2, pp. 243-247. https://doi.org/10.1006/exer.1993.1120
Kumari K, Ansari N, Saxena M, Awasthi YC, Srivastava S. Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens. Experimental Eye Research. 1993 Aug;57(2):243-247. https://doi.org/10.1006/exer.1993.1120
Kumari, Kshama ; Ansari, Naseem ; Saxena, Manju ; Awasthi, Yogesh C. ; Srivastava, Satish. / Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens. In: Experimental Eye Research. 1993 ; Vol. 57, No. 2. pp. 243-247.
@article{2c5fa4e88ade4fb0a8b5a84fd6ae6dbe,
title = "Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens",
abstract = "Dinitrophenyl S-glutathione (Dnp-SG) ATPase which catalyses the hydrolysis of ATP in the presence of GSH-conjugates has been implicated previously in the transport of these conjugates. In the present studies we demonstrate that Dnp-SG ATPase is present in bovine lens epithelium and cortex. The specific activity per mg membrane protein was found to be 75-fold higher in the epithelium as compared to the cortex. No enzyme was detected in the nuclear region of the lens. Dnp-SG ATPase was purified from bovine lens epithelium and cortex using Dnp-SG-Sepharose 6MB affinity chromatography. The partially purified Dnp-SG ATPase had two distinct Km values, 120 μM and 1·0 mM. The antibodies raised against human erythrocyte Dnp-SG ATPase cross-reacted with the bovine lens epithelium Dnp-SG ATPase which was identified by Western blot as a band corresponding to an approximate Mr value of 80000 Da.",
keywords = "bovine lens, Dnp-SG ATPase, glutathione, glutathione conjugates, xenobiotic transport",
author = "Kshama Kumari and Naseem Ansari and Manju Saxena and Awasthi, {Yogesh C.} and Satish Srivastava",
year = "1993",
month = "8",
doi = "10.1006/exer.1993.1120",
language = "English (US)",
volume = "57",
pages = "243--247",
journal = "Experimental Eye Research",
issn = "0014-4835",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Low and High Km Forms of R;Regular Article Dinitrophenylglutathione-stimulated ATPase in Bovine Lens

AU - Kumari, Kshama

AU - Ansari, Naseem

AU - Saxena, Manju

AU - Awasthi, Yogesh C.

AU - Srivastava, Satish

PY - 1993/8

Y1 - 1993/8

N2 - Dinitrophenyl S-glutathione (Dnp-SG) ATPase which catalyses the hydrolysis of ATP in the presence of GSH-conjugates has been implicated previously in the transport of these conjugates. In the present studies we demonstrate that Dnp-SG ATPase is present in bovine lens epithelium and cortex. The specific activity per mg membrane protein was found to be 75-fold higher in the epithelium as compared to the cortex. No enzyme was detected in the nuclear region of the lens. Dnp-SG ATPase was purified from bovine lens epithelium and cortex using Dnp-SG-Sepharose 6MB affinity chromatography. The partially purified Dnp-SG ATPase had two distinct Km values, 120 μM and 1·0 mM. The antibodies raised against human erythrocyte Dnp-SG ATPase cross-reacted with the bovine lens epithelium Dnp-SG ATPase which was identified by Western blot as a band corresponding to an approximate Mr value of 80000 Da.

AB - Dinitrophenyl S-glutathione (Dnp-SG) ATPase which catalyses the hydrolysis of ATP in the presence of GSH-conjugates has been implicated previously in the transport of these conjugates. In the present studies we demonstrate that Dnp-SG ATPase is present in bovine lens epithelium and cortex. The specific activity per mg membrane protein was found to be 75-fold higher in the epithelium as compared to the cortex. No enzyme was detected in the nuclear region of the lens. Dnp-SG ATPase was purified from bovine lens epithelium and cortex using Dnp-SG-Sepharose 6MB affinity chromatography. The partially purified Dnp-SG ATPase had two distinct Km values, 120 μM and 1·0 mM. The antibodies raised against human erythrocyte Dnp-SG ATPase cross-reacted with the bovine lens epithelium Dnp-SG ATPase which was identified by Western blot as a band corresponding to an approximate Mr value of 80000 Da.

KW - bovine lens

KW - Dnp-SG ATPase

KW - glutathione

KW - glutathione conjugates

KW - xenobiotic transport

UR - http://www.scopus.com/inward/record.url?scp=0027338309&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027338309&partnerID=8YFLogxK

U2 - 10.1006/exer.1993.1120

DO - 10.1006/exer.1993.1120

M3 - Article

C2 - 8405191

AN - SCOPUS:0027338309

VL - 57

SP - 243

EP - 247

JO - Experimental Eye Research

JF - Experimental Eye Research

SN - 0014-4835

IS - 2

ER -

Access to Document