caa a22 4500 477118623 CHVBK 20180405111629.0 cr unu---uuuuu 170330e19960901xx s 000 0 eng 10.1007/BF00426330 doi (NATIONALLICENCE)springer-10.1007/BF00426330 Occurrence of histone-related oxalate binding in rat liver nucleus [Elektronische Daten] [Ramasamy Selvam, Vadlamudi Prasanna Lakshmi] The rat liver nuclear oxalate binding protein was isolated, purified by anion and cation exchange column chromatography using Diethyl Amino Ethyl Sephadex, Carboxy Methyl Cellulose and Carboxy Methyl Sephadex C-50 ion exchangers. The purified oxalate binding protein was found to be H1B of H1 fraction of histories. Kinetic analysis of oxalate binding showed the presence of two affinity sites, one with Kd of 133.5 nM and Bmax of 40 pmoles and another with Kd of 262.5 nM and Bmax of 210 pmoles. The optimal oxalate binding was at pH 4.2 and at 28°C. The oxalate binding was specific and reversible and not due to ionic charge interaction. The IC50 of other dicarboxylates was higher than that of oxalate. EGTA had no effect on oxalate binding but di- and tri-carboxylate carrier inhibitors and thiol modifying agents significantly lowered the binding activity. Oxalate binding to histones was significantly reduced in the presence of DNA or nucleotides, but RNA had no effect. ATP completely inhibited the oxalate binding activity at 1 mM concentration. Different tissues exhibited oxalate binding showing ubiquitous nature. Calf thymus H1 showed maximal binding similar to liver histones. Kluwer Academic Publishers, 1996 rat liver nucleus nationallicence oxalate binding protein nationallicence histone III nationallicence purification nationallicence kinetics nationallicence ADP : Adenosine diphosphate nationallicence ATP : Adenosine triphosphate nationallicence DNA : Deoxyribonucleic acid nationallicence RNA : Ribonucleic acid nationallicence Selvam Ramasamy Department of Medical Biochemistry, Dr. A.L.M. Post Graduate Institute of Basic Medical Sciences, University of Madras, 600 113, Taramani, Madras, India aut Prasanna Lakshmi Vadlamudi Department of Medical Biochemistry, Dr. A.L.M. Post Graduate Institute of Basic Medical Sciences, University of Madras, 600 113, Taramani, Madras, India aut Molecular and Cellular Biochemistry Kluwer Academic Publishers 156/2(1996-09-01), 93-100 0300-8177 156:2<93 1996 156 11010 https://doi.org/10.1007/BF00426330 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00426330 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Selvam Ramasamy Department of Medical Biochemistry, Dr. A.L.M. Post Graduate Institute of Basic Medical Sciences, University of Madras, 600 113, Taramani, Madras, India aut NATIONALLICENCE 700 1- Prasanna Lakshmi Vadlamudi Department of Medical Biochemistry, Dr. A.L.M. Post Graduate Institute of Basic Medical Sciences, University of Madras, 600 113, Taramani, Madras, India aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers 156/2(1996-09-01), 93-100 0300-8177 156:2<93 1996 156 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer