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 language | English (US) |
---|---|
Pages (from-to) | 243-247 |
Number of pages | 5 |
Journal | Experimental Eye Research |
Volume | 57 |
Issue number | 2 |
DOIs | |
State | Published - Aug 1993 |
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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
}
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
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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 -