메뉴 건너뛰기




Volumn 16, Issue 2, 2009, Pages 173-181

Purification and characterization of an anticalcifying protein from the seeds of Trachyspermum ammi (L.)

Author keywords

Anticalcifying; Calcium oxalate; Inhibitory protein; Trachyspermum ammi; Urolithiasis

Indexed keywords

CALCIUM OXALATE;

EID: 63449121314     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609787316252     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 0029023254 scopus 로고    scopus 로고
    • Schroder, F.H. Association of calcium oxalate monohydrate crystals with MDCK cells. (1995) Kidney Int., 48, 129.
    • Schroder, F.H. Association of calcium oxalate monohydrate crystals with MDCK cells. (1995) Kidney Int., 48, 129.
  • 3
    • 0345305852 scopus 로고    scopus 로고
    • Moghadam, M.F., Tandon, C., Aggarwal, S., Singla, S.K., Singh, S.K., Sharma, S.K., Varshney, G.C. and Jethi, R.K. Concentration of a potent calcium oxalate monohydrate crystal growth inhibitor in the urine of normal persons and kidney stone patients by ELISA-based assay system employing monoclonal antibodies. (2003) J. Cell. Biochem., 90, 1261.
    • Moghadam, M.F., Tandon, C., Aggarwal, S., Singla, S.K., Singh, S.K., Sharma, S.K., Varshney, G.C. and Jethi, R.K. Concentration of a potent calcium oxalate monohydrate crystal growth inhibitor in the urine of normal persons and kidney stone patients by ELISA-based assay system employing monoclonal antibodies. (2003) J. Cell. Biochem., 90, 1261.
  • 4
    • 28244452022 scopus 로고    scopus 로고
    • Aggarwal, S., Tandon, C., Forouzandeh, M., Singla, S.K., Kiran, R. and Jethi, R.K. Role of a protein inhibitor isolated from human renal stone matrix in urolithia. (2005) Indian J. Biochem. Biophy., 42, 113.
    • Aggarwal, S., Tandon, C., Forouzandeh, M., Singla, S.K., Kiran, R. and Jethi, R.K. Role of a protein inhibitor isolated from human renal stone matrix in urolithia. (2005) Indian J. Biochem. Biophy., 42, 113.
  • 5
    • 0033898884 scopus 로고    scopus 로고
    • Aggarwal, S., Tandon, C., Forouzandeh, M., Singla, S.K., Kiran, R. and Jethi, R.K. Role of biomolecules from human renal stone matrix on COM crystal growth. (2000) Mol. Cell. Biochem., 210, 109.
    • Aggarwal, S., Tandon, C., Forouzandeh, M., Singla, S.K., Kiran, R. and Jethi, R.K. Role of biomolecules from human renal stone matrix on COM crystal growth. (2000) Mol. Cell. Biochem., 210, 109.
  • 6
    • 0032031489 scopus 로고    scopus 로고
    • Tandon, C., Aggarwal, S., Forouzandeh, M. and Jethi, R.K. Inhibitors of in vitro mineralization from rabbit aorta and their role in biomineralization. (1998) J. Cell. Biochem., 68, 287.
    • Tandon, C., Aggarwal, S., Forouzandeh, M. and Jethi, R.K. Inhibitors of in vitro mineralization from rabbit aorta and their role in biomineralization. (1998) J. Cell. Biochem., 68, 287.
  • 7
    • 0029125269 scopus 로고    scopus 로고
    • Hoyer, J.R., Otvos, L. Jr. and Urge, L. Osteopontin in urinary stone formation. (1995) Ann. N. Y. Acad. Sci.,760, 257.
    • Hoyer, J.R., Otvos, L. Jr. and Urge, L. Osteopontin in urinary stone formation. (1995) Ann. N. Y. Acad. Sci.,760, 257.
  • 8
    • 36549048941 scopus 로고    scopus 로고
    • Terlecki, R.P. and Triest, J.A. A contemporary evaluation of the auditory hazard of extracorporeal shock wave lithotripsy. (2007) Urology, 70, 898.
    • Terlecki, R.P. and Triest, J.A. A contemporary evaluation of the auditory hazard of extracorporeal shock wave lithotripsy. (2007) Urology, 70, 898.
  • 9
    • 34548187445 scopus 로고    scopus 로고
    • Li, X., He, D., Zhang, L., Xue, Y, Cheng, X. and Luo, Y. Pyrrolidine dithiocarbamate attenuates shock wave induced MDCK cells injury via inhibiting nuclear factor-kappa B activation. (2007) Urol. Res., 35, 193.
    • Li, X., He, D., Zhang, L., Xue, Y, Cheng, X. and Luo, Y. Pyrrolidine dithiocarbamate attenuates shock wave induced MDCK cells injury via inhibiting nuclear factor-kappa B activation. (2007) Urol. Res., 35, 193.
  • 10
    • 63449116299 scopus 로고    scopus 로고
    • Moran, M.E., Hynynen, K., Bottaccini, M.R. and Drach, G.W. Cavitation and thermal phenomena associated with high energy shock waves-in vitro and in vivo measurements. (1990) J. Urol., 142, 388.
    • Moran, M.E., Hynynen, K., Bottaccini, M.R. and Drach, G.W. Cavitation and thermal phenomena associated with high energy shock waves-in vitro and in vivo measurements. (1990) J. Urol., 142, 388.
  • 11
    • 0026331419 scopus 로고    scopus 로고
    • Suhr, D., Brummer, F. and Hulser, D.F. Cavitation-generated free radicals during shock wave exposure: Investigations with cell-free solutions and suspended cells. (1991) Ultrasound Med. Biol., 17, 761.
    • Suhr, D., Brummer, F. and Hulser, D.F. Cavitation-generated free radicals during shock wave exposure: Investigations with cell-free solutions and suspended cells. (1991) Ultrasound Med. Biol., 17, 761.
  • 12
    • 0020821642 scopus 로고    scopus 로고
    • Jethi, R.K., Duggal, B., Sahota, R.S., Gupta, M. and Sofat, LB. Effect of the aqueous extract of an Ayurvedic compound preparation on mineralization & demineralization reactions. (1983) Indian J. Med. Res., 78, 422.
    • Jethi, R.K., Duggal, B., Sahota, R.S., Gupta, M. and Sofat, LB. Effect of the aqueous extract of an Ayurvedic compound preparation on mineralization & demineralization reactions. (1983) Indian J. Med. Res., 78, 422.
  • 13
    • 0037292639 scopus 로고    scopus 로고
    • Barros, M.E., Schor, N. and Boim, M.A. Effect of an aqueous extract from P. niruri on calcium oxalate crystallization in vitro. (2003) Urol. Res., 30, 374.
    • Barros, M.E., Schor, N. and Boim, M.A. Effect of an aqueous extract from P. niruri on calcium oxalate crystallization in vitro. (2003) Urol. Res., 30, 374.
  • 14
    • 33749486804 scopus 로고    scopus 로고
    • Grases, F., Costa-Bauza, A. and Prieto, R.M. Renal lithiasis and nutrition. (2006) Nutr. J., 5, 23.
    • Grases, F., Costa-Bauza, A. and Prieto, R.M. Renal lithiasis and nutrition. (2006) Nutr. J., 5, 23.
  • 17
    • 29244487146 scopus 로고    scopus 로고
    • Christina, A.J., Ashok, K., Packialakshmi, M., Tobin, G.C., Preethi, J. and Murugesh, N. Antilithiatic effect of Asparagus racemosus willd on ethylene glycol induced lithiasis in male albino Wistar rats. (2005) Methods Find. Exp. Clin. Pharmacol, 27, 633.
    • Christina, A.J., Ashok, K., Packialakshmi, M., Tobin, G.C., Preethi, J. and Murugesh, N. Antilithiatic effect of Asparagus racemosus willd on ethylene glycol induced lithiasis in male albino Wistar rats. (2005) Methods Find. Exp. Clin. Pharmacol, 27, 633.
  • 18
    • 4544243071 scopus 로고    scopus 로고
    • Atmani, F., Farell, G. and Lieske, J.C. Extract from Herniaria hirsuta coats calcium oxalate monohydrate crystals and blocks their adhesion to renal epithelial cells. (2004) J. Urol, 172, 1510.
    • Atmani, F., Farell, G. and Lieske, J.C. Extract from Herniaria hirsuta coats calcium oxalate monohydrate crystals and blocks their adhesion to renal epithelial cells. (2004) J. Urol, 172, 1510.
  • 19
    • 21544439028 scopus 로고    scopus 로고
    • Joshi, V.S., Parekh, B.B., Joshi, M.J. and Vaidya, A.D. Inhibition of the growth of urinary calcium hydrogen phosphate dihydrate crystals with aqueous extracts of Tribulus terrestris and Bergenia ligulata. (2005) Urol. Res., 33, 80.
    • Joshi, V.S., Parekh, B.B., Joshi, M.J. and Vaidya, A.D. Inhibition of the growth of urinary calcium hydrogen phosphate dihydrate crystals with aqueous extracts of Tribulus terrestris and Bergenia ligulata. (2005) Urol. Res., 33, 80.
  • 20
    • 31044450826 scopus 로고    scopus 로고
    • Chutipongtanate, S., Nakagawa, Y., Sritippayawan, S., Pittayamateekul, J., Parichatikanond, P., Westley, B.R., May, F.E., Malasit, P. and Thongboonkerd, V. Identification of human urinary trefoil factor 1 as a novel calcium oxalate crystal growth inhibitor. (2005) J. Clin. Invest., 115, 3613.
    • Chutipongtanate, S., Nakagawa, Y., Sritippayawan, S., Pittayamateekul, J., Parichatikanond, P., Westley, B.R., May, F.E., Malasit, P. and Thongboonkerd, V. Identification of human urinary trefoil factor 1 as a novel calcium oxalate crystal growth inhibitor. (2005) J. Clin. Invest., 115, 3613.
  • 21
    • 0018080580 scopus 로고    scopus 로고
    • Nakagawa, Y., Kaiser, E.T. and Coe, F.L. Isolation and characterization of calcium oxalate crystal growth inhibitors from human urine. (1978) Biochem. Biophys. Res. Commun., 84, 1038.
    • Nakagawa, Y., Kaiser, E.T. and Coe, F.L. Isolation and characterization of calcium oxalate crystal growth inhibitors from human urine. (1978) Biochem. Biophys. Res. Commun., 84, 1038.
  • 22
    • 4243054286 scopus 로고    scopus 로고
    • Trinder, P. Colorimetric microdetermination of calcium in serum. (1960) Analyst, 85, 889.
    • Trinder, P. Colorimetric microdetermination of calcium in serum. (1960) Analyst, 85, 889.
  • 23
    • 63449125803 scopus 로고    scopus 로고
    • Gomori, H.D. A modifiaction of colorimetric phosphorous determination for use with photoelectric colorimeter. (1941) J. Lab. Clin. Med., 27, 955.
    • Gomori, H.D. A modifiaction of colorimetric phosphorous determination for use with photoelectric colorimeter. (1941) J. Lab. Clin. Med., 27, 955.
  • 24
    • 0014949207 scopus 로고    scopus 로고
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. (1970) Nature, 227, 680.
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. (1970) Nature, 227, 680.
  • 25
    • 63449129410 scopus 로고    scopus 로고
    • Elkin, R.G. and Wasynczuk, A. M. Amino acid analysis of feedstuff hydrolysates by precolumn derivatization with phenylisothiocyanate and reversed-phase high-performance liquid chromatography. (1987) Cereal. Chem., 64, 226.
    • Elkin, R.G. and Wasynczuk, A. M. Amino acid analysis of feedstuff hydrolysates by precolumn derivatization with phenylisothiocyanate and reversed-phase high-performance liquid chromatography. (1987) Cereal. Chem., 64, 226.
  • 26
    • 0022426042 scopus 로고    scopus 로고
    • Yang, V.C. and Langer, R. pH-dependent binding analysis, a new and rapid method for isoelectric point estimation. (1985) Anal. Biochem., 147, 148.
    • Yang, V.C. and Langer, R. pH-dependent binding analysis, a new and rapid method for isoelectric point estimation. (1985) Anal. Biochem., 147, 148.
  • 27
    • 63449092960 scopus 로고    scopus 로고
    • Pearl, F.M., Martin, N., Bray, J.E., Buchan, D.W., Harrison, A.P., Lee, D., Reeves, G.A., Shepherd, A.J., Sillitoe, I., Todd, A.E., Thornton, J.M. and Orengo, C.A. A rapid classification protocol for the CATH Domain Database to support structural genomics. (1997) Nucleic Acids Res., 25, 3389.
    • Pearl, F.M., Martin, N., Bray, J.E., Buchan, D.W., Harrison, A.P., Lee, D., Reeves, G.A., Shepherd, A.J., Sillitoe, I., Todd, A.E., Thornton, J.M. and Orengo, C.A. A rapid classification protocol for the CATH Domain Database to support structural genomics. (1997) Nucleic Acids Res., 25, 3389.
  • 28
    • 0032568655 scopus 로고    scopus 로고
    • Schultz, J., Milpetz, F., Bork, P. and Ponting, C.P. SMART, a simple modular architecture research tool: identification of signaling domains. (1998) Proc. Natl. Acad. Sci. USA, 95, 5857.
    • Schultz, J., Milpetz, F., Bork, P. and Ponting, C.P. SMART, a simple modular architecture research tool: identification of signaling domains. (1998) Proc. Natl. Acad. Sci. USA, 95, 5857.
  • 29
    • 33644877451 scopus 로고    scopus 로고
    • Letunic, I., Copley, R.R., Pils, B., Pinkert, S., Schultz, J. and Bork, P. SMART 5: domains in the context of genomes and networks. (2006) Nucleic Acids Res., 34, 257.
    • Letunic, I., Copley, R.R., Pils, B., Pinkert, S., Schultz, J. and Bork, P. SMART 5: domains in the context of genomes and networks. (2006) Nucleic Acids Res., 34, 257.
  • 30
    • 71849104860 scopus 로고    scopus 로고
    • Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. Protein measurement with the folin phenol reagent. (1951) J. Biol. Chem., 193, 265.
    • Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. Protein measurement with the folin phenol reagent. (1951) J. Biol. Chem., 193, 265.
  • 31
    • 0026467489 scopus 로고    scopus 로고
    • Hess, B. Tamm-Horsfall glycoprotein inhibitor or promoter of calcium oxalate monohydrate crystallization processes. (1992) Urol. Res., 20, 83.
    • Hess, B. Tamm-Horsfall glycoprotein inhibitor or promoter of calcium oxalate monohydrate crystallization processes. (1992) Urol. Res., 20, 83.
  • 32
    • 0026571598 scopus 로고    scopus 로고
    • Shiraga, H., Min, W., VanDusen, W.J., Clayman, M.D., Miner, D., Terrell, C.H., Sherbotie, J.R., Foreman, J.W., Przysiecki, C. and Neilson, E.G. Inhibition of calcium oxalate crystal growth in vitro by uropontin: another member of the aspartic acid-rich protein superfamily. (1992) Proc. Natl. Acad. Sci. USA, 89, 426.
    • Shiraga, H., Min, W., VanDusen, W.J., Clayman, M.D., Miner, D., Terrell, C.H., Sherbotie, J.R., Foreman, J.W., Przysiecki, C. and Neilson, E.G. Inhibition of calcium oxalate crystal growth in vitro by uropontin: another member of the aspartic acid-rich protein superfamily. (1992) Proc. Natl. Acad. Sci. USA, 89, 426.
  • 33
    • 85190690302 scopus 로고    scopus 로고
    • Atmani, F. and Khan S.R. Role of urinary bikunin in the inhibition of calcium oxalate crystallization. (1999) J. Am. Soc. Nephrol, 10, S385.
    • Atmani, F. and Khan S.R. Role of urinary bikunin in the inhibition of calcium oxalate crystallization. (1999) J. Am. Soc. Nephrol, 10, S385.
  • 34
    • 0032725933 scopus 로고    scopus 로고
    • Webb, M.A. Cell mediated crystallization of calcium oxalate in plants. (1999) Plant Cell, 11, 751.
    • Webb, M.A. Cell mediated crystallization of calcium oxalate in plants. (1999) Plant Cell, 11, 751.
  • 35
    • 0037680190 scopus 로고    scopus 로고
    • Nakata, P.A. Advances in our understanding of calcium oxalate crystal formation and function in plants. (2003) Plant Sci., 164, 901.
    • Nakata, P.A. Advances in our understanding of calcium oxalate crystal formation and function in plants. (2003) Plant Sci., 164, 901.
  • 36
    • 0142245630 scopus 로고    scopus 로고
    • Li, X., Zhang, D., Lynch-Holm, V.J., Okita, T.W. and Franceschi, V.R. Isolation of a crystal matrix protein associated with calcium oxalate precipitation in vacuoles of specialized cells. (2003) Plant Physiol, 133, 549.
    • Li, X., Zhang, D., Lynch-Holm, V.J., Okita, T.W. and Franceschi, V.R. Isolation of a crystal matrix protein associated with calcium oxalate precipitation in vacuoles of specialized cells. (2003) Plant Physiol, 133, 549.
  • 37
    • 0021796043 scopus 로고    scopus 로고
    • Addadi, L. and Weiner S. Interactions between acid proteins and crystals: stereochemical requirements in biomineralization. (1985) Proc. Natl. Acad. Sci. USA, 82, 4110.
    • Addadi, L. and Weiner S. Interactions between acid proteins and crystals: stereochemical requirements in biomineralization. (1985) Proc. Natl. Acad. Sci. USA, 82, 4110.
  • 38
    • 15744379077 scopus 로고    scopus 로고
    • Jáuregui-Zúñiga, D., Reyes-Grajeda, J.P. and Moreno, A. Modifications on the morphology of synthetically-grown calcium oxalate crystals by crystal-associated proteins isolated from bean seed coats (Phaseolus vulgaris). (2005) Plant Sci., 168, 1163.
    • Jáuregui-Zúñiga, D., Reyes-Grajeda, J.P. and Moreno, A. Modifications on the morphology of synthetically-grown calcium oxalate crystals by crystal-associated proteins isolated from bean seed coats (Phaseolus vulgaris). (2005) Plant Sci., 168, 1163.
  • 39
    • 0034003727 scopus 로고    scopus 로고
    • Arnott, H.J. and Webb, M.A. Twinned Raphides of Calcium Oxalate in Grape (Vitis): Implications for Crystal Stability and Function. (2000) Int. J. Plant Sci., 161, 133.
    • Arnott, H.J. and Webb, M.A. Twinned Raphides of Calcium Oxalate in Grape (Vitis): Implications for Crystal Stability and Function. (2000) Int. J. Plant Sci., 161, 133.
  • 40
    • 34848886909 scopus 로고    scopus 로고
    • Jaillon, O, Aury, J.M, Noel, B, Policriti, A, Clepet, C, Casagrande, A, Choisne, N, Aubourg, S, Vitulo, N, Jubin, C, Vezzi, A, Legeai, F, Hugueney, P, Dasilva, C, Horner, D, Mica, E, Jublot, D, Poulain, J, Bruyère, C, Billault, A, Segurens, B, Gouyvenoux, M, Ugarte, E, Cattonaro, F, Anthouard, V, Vico, V, Del Fabbro, C, Alaux, M, Di Gaspero, G, Dumas, V, Felice, N, Paillard, S, Juman, I, Moroldo, M, Scalabrin, S, Canaguier, A, Le Clainche, I, Malacrida, G, Durand, E, Pesole, G, Laucou, V, Chatelet, P, Merdinoglu, D, Delledonne, M, Pezzotti, M, Lecharny, A, Scarpelli, C, Artiguenave, F, Pè, M.E, Valle, G, Morgante, M, Caboche, M, Adam-Blondon, A.F, Weissenbach, J, Quétier, F. and Wincker, P. The grapevine genome sequence suggests ancestral hexaploidization in major angiosperm phyla, 2007 Nature, 449, 463
    • Jaillon, O., Aury, J.M., Noel, B., Policriti, A., Clepet, C., Casagrande, A., Choisne, N., Aubourg, S., Vitulo, N., Jubin, C., Vezzi, A., Legeai, F., Hugueney, P., Dasilva, C., Horner, D., Mica, E., Jublot, D., Poulain, J., Bruyère, C., Billault, A., Segurens, B., Gouyvenoux, M., Ugarte, E., Cattonaro, F., Anthouard, V., Vico, V., Del Fabbro, C., Alaux, M., Di Gaspero, G., Dumas, V., Felice, N., Paillard, S., Juman, I., Moroldo, M., Scalabrin, S., Canaguier, A., Le Clainche, I., Malacrida, G., Durand, E., Pesole, G., Laucou, V., Chatelet, P., Merdinoglu, D., Delledonne, M., Pezzotti, M., Lecharny, A., Scarpelli, C., Artiguenave, F., Pè, M.E., Valle, G., Morgante, M., Caboche, M., Adam-Blondon, A.F., Weissenbach, J., Quétier, F. and Wincker, P. The grapevine genome sequence suggests ancestral hexaploidization in major angiosperm phyla. (2007) Nature, 449, 463.
  • 41
    • 0024396312 scopus 로고    scopus 로고
    • Strynadka, N.C.J. and James, M.N.G. Crystal structures of the helix-loop-helix calcium-binding proteins. (1989) Annu. Rev. Biochem., 58,951.
    • Strynadka, N.C.J. and James, M.N.G. Crystal structures of the helix-loop-helix calcium-binding proteins. (1989) Annu. Rev. Biochem., 58,951.
  • 42
    • 0022001045 scopus 로고    scopus 로고
    • Herzberg, O. and James M.N.G. Structure of the calcium regulatory muscle protein troponin-C at 2.8Å resolution. (1985) Nature, 313, 653.
    • Herzberg, O. and James M.N.G. Structure of the calcium regulatory muscle protein troponin-C at 2.8Å resolution. (1985) Nature, 313, 653.
  • 43
    • 85176636980 scopus 로고    scopus 로고
    • Mustafi, D. and Nakagawa, Y. Characterization of calcium-binding sites in the kidney stone inhibitor glycoprotein nephrocalcin with vanadyl ions: Electron paramagnetic resonance and electron nuclear double resonance spectroscopy. (1994) Proc. Natl. Acad. Sci. USA, 91, 11323.
    • Mustafi, D. and Nakagawa, Y. Characterization of calcium-binding sites in the kidney stone inhibitor glycoprotein nephrocalcin with vanadyl ions: Electron paramagnetic resonance and electron nuclear double resonance spectroscopy. (1994) Proc. Natl. Acad. Sci. USA, 91, 11323.
  • 44
    • 0031847270 scopus 로고    scopus 로고
    • Pillay, S.N., Asplin, J.R. and Coe, F.L. Evidence that calgranulin is produced by kidney cells and is an inhibitor of calcium oxalate crystallization. (1998) Am. J. physiol Ren. Physiol, 44, F255.
    • Pillay, S.N., Asplin, J.R. and Coe, F.L. Evidence that calgranulin is produced by kidney cells and is an inhibitor of calcium oxalate crystallization. (1998) Am. J. physiol Ren. Physiol, 44, F255.
  • 45
    • 0028134998 scopus 로고    scopus 로고
    • DellAngelica, E.C., Schleicher, C.H. and Santome, J.A. Primary structure and binding properties of calgranulin C., a novel S100-like calcium-binding protein from pig granulocytes. (1994) J. Biol. Chem., 269, 28929.
    • DellAngelica, E.C., Schleicher, C.H. and Santome, J.A. Primary structure and binding properties of calgranulin C., a novel S100-like calcium-binding protein from pig granulocytes. (1994) J. Biol. Chem., 269, 28929.
  • 46
    • 0030995856 scopus 로고    scopus 로고
    • Hohenester, E., Maurer, P. and Timp, R. Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. (1997) EMBO. J., 16, 3778.
    • Hohenester, E., Maurer, P. and Timp, R. Crystal structure of a pair of follistatin-like and EF-hand calcium-binding domains in BM-40. (1997) EMBO. J., 16, 3778.
  • 47
    • 0025021153 scopus 로고    scopus 로고
    • Kohri, K., Umekawa, T., Kodama, M., Katayama, Y., Ishikawa, Y., Takada, M., Katoh, Y., Kataoka, K., Iguchi, M. and Kurita, T. Inhibitory effect of glutamic acid and aspartic acid on calcium oxalate crystal formation. (1990) Eur. Urol, 17, 173.
    • Kohri, K., Umekawa, T., Kodama, M., Katayama, Y., Ishikawa, Y., Takada, M., Katoh, Y., Kataoka, K., Iguchi, M. and Kurita, T. Inhibitory effect of glutamic acid and aspartic acid on calcium oxalate crystal formation. (1990) Eur. Urol, 17, 173.
  • 48
    • 63449111377 scopus 로고    scopus 로고
    • Gul, A. and Peter, R. Models for protein to bind calcium oxalate surfaces. (2007) Urol. Res., 35, 65.
    • Gul, A. and Peter, R. Models for protein to bind calcium oxalate surfaces. (2007) Urol. Res., 35, 65.
  • 49
    • 33748564957 scopus 로고    scopus 로고
    • Wang, L., Qiu, S.R., Zachowicz, W., Guan, X., Deyoreo, J.J., Nancollas, G.H. and Hoyer J.R. Modulation of calcium oxalate crystallization by linear aspartic acid-rich peptides. (2006) Langmuir, 22, 7279.
    • Wang, L., Qiu, S.R., Zachowicz, W., Guan, X., Deyoreo, J.J., Nancollas, G.H. and Hoyer J.R. Modulation of calcium oxalate crystallization by linear aspartic acid-rich peptides. (2006) Langmuir, 22, 7279.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.