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Volumn 7, Issue 1, 2011, Pages 79-83

Effects of ceftazidime pentahydrate, prednisolone, amikacin sulfate, ceftriaxone sodium and teicoplanin on bovine milk lactoperoxidase activity

Author keywords

Antibiotics; Bovine milk; Enzyme inhibition; Lactoperoxidase; LPO

Indexed keywords

2,2' AZINOBIS(3 ETHYLBENZOTHIAZOLINE 6 SULFONIC ACID); AMIKACIN; CEFTAZIDIME; CEFTRIAXONE; LACTOPEROXIDASE; PREDNISOLONE; TEICOPLANIN;

EID: 78649422585     PISSN: 18117775     EISSN: 18125700     Source Type: Journal    
DOI: 10.3923/ijp.2011.79.83     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 8844243391 scopus 로고    scopus 로고
    • Effects of ceftriaxone sodium on in vitro gallbladder contractility in guinea pigs
    • Arpacik, M., C. Ceran, T. Kaya, B. Karadas, B. Sarac and G. Koyluoglu, 2004. Effects of ceftriaxone sodium on in vitro gallbladder contractility in guinea pigs. J. Surg. Res., 122: 157-161.
    • (2004) J. Surg. Res. , vol.122 , pp. 157-161
    • Arpacik, M.1    Ceran, C.2    Kaya, T.3    Karadas, B.4    Sarac, B.5    Koyluoglu, G.6
  • 2
    • 2942582777 scopus 로고    scopus 로고
    • Effect of melatonin on carbonic anhydrase from human erythrocyte in vitro and from rat erythrocyte in vivo
    • Beydemir, S. and I Gulcin, 2004. Effect of melatonin on carbonic anhydrase from human erythrocyte in vitro and from rat erythrocyte in vivo. J. Enzym. Inhib. Med. Chem., 19: 193-197.
    • (2004) J. Enzym. Inhib. Med. Chem. , vol.19 , pp. 193-197
    • Beydemir, S.1    Gulcin, I.2
  • 3
    • 0348218170 scopus 로고    scopus 로고
    • Glucose 6-phosphate dehydrogenase: In vitro and yn vivo effects of dantrolene sodium
    • Beydemir, S., I. Gulcin, O.I. Kufrevioglu and M. Ciftci, 2003. Glucose 6-phosphate dehydrogenase: In vitro and yn vivo effects of dantrolene sodium. Pol. J. Pharmacol, 55: 787-792.
    • (2003) Pol. J. Pharmacol. , vol.55 , pp. 787-792
    • Beydemir, S.1    Gulcin, I.2    Kufrevioglu, O.I.3    Ciftci, M.4
  • 5
    • 33748304355 scopus 로고    scopus 로고
    • Lactoperoxidase: From catalytic mechanism to practical applications
    • Boots, J.W. and R. Floris, 2006. Lactoperoxidase: From catalytic mechanism to practical applications. Int. Dairy J., 16: 1272-1276.
    • (2006) Int. Dairy J. , vol.16 , pp. 1272-1276
    • Boots, J.W.1    Floris, R.2
  • 6
    • 34548311972 scopus 로고    scopus 로고
    • Lactoperoxidase folding and catalysis relies on the stabilization of the â-helix rich core domain: A thermal unfolding study
    • Boscolo, B., S.S. Leal, E.M. Ghibaudi and CM. Gomes, 2007. Lactoperoxidase folding and catalysis relies on the stabilization of the â-helix rich core domain: A thermal unfolding study. Biochim. Biophys. Acta, 1774: 1164-1172.
    • (2007) Biochim. Biophys. Acta. , pp. 1164-1172
    • Boscolo, B.1    Leal, S.S.2    Ghibaudi, E.M.3    Gomes, C.M.4
  • 7
    • 0017200001 scopus 로고
    • Effects of enzyme induction on metabolism of prednisolone
    • Brooks, P.M., M. Grove and W.W. Downie, 1976. Effects of enzyme induction on metabolism of prednisolone. Ann. Rheum. Dis., 35: 339-343.
    • (1976) Ann. Rheum. Dis. , vol.35 , pp. 339-343
    • Brooks, P.M.1    Grove, M.2    Downie, W.W.3
  • 9
    • 40949140542 scopus 로고    scopus 로고
    • The inhibitory effect of ethanol on carbonic anhydrase isoenzymes: In vivo and in vitro studies
    • Coban T.A., S. Beydemir, I. Gulcin and D. Ekinci, 2008. The inhibitory effect of ethanol on carbonic anhydrase isoenzymes: In vivo and in vitro studies. J. Enzym. Inhib. Med. Chem., 23: 266-270.
    • (2008) J. Enzym. Inhib. Med. Chem. , vol.23 , pp. 266-270
    • Coban, T.A.1    Beydemir, S.2    Gulcin, I.3    Ekinci, D.4
  • 10
    • 36849015851 scopus 로고    scopus 로고
    • Morphine inhibits erythrocyte carbonic anhydrase in vitro and in vivo
    • Coban, T.A., S. Beydemir, I. Gulcin and D. Ekmci, 2007. Morphine inhibits erythrocyte carbonic anhydrase in vitro and in vivo. Biol. Pharm. Bull., 30: 2257-2261.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 2257-2261
    • Coban, T.A.1    Beydemir, S.2    Gulcin, I.3    Ekmci, D.4
  • 12
    • 0021100329 scopus 로고
    • Identification, purification and characterization of a non-heme lactoperoxidase in bovine milk
    • Dumontet, C. and B. Rousset, 1983. Identification, purification and characterization of a non-heme lactoperoxidase in bovine milk. J. Biol. Chem., 258: 14166-14172.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14166-14172
    • Dumontet, C.1    Rousset, B.2
  • 13
    • 0032982629 scopus 로고    scopus 로고
    • Stability of reconstituted solutions of ceftazidime for injections: An HPLC and CE approach
    • Farina, A., R. Porra, V. Cotichim and A. Doldo, 1999. Stability of reconstituted solutions of ceftazidime for injections: An HPLC and CE approach. J. Pharm. Biomed. Anal, 20: 521-530.
    • (1999) J. Pharm. Biomed. Anal. , vol.20 , pp. 521-530
    • Farina, A.1    Porra, R.2    Cotichim, V.3    Doldo, A.4
  • 15
    • 0016792693 scopus 로고
    • Lactoperoxidase activity in human milk and in saliva of newborn infants
    • Gothefors, L. and S. Marklund, 1975. Lactoperoxidase activity in human milk and in saliva of newborn infants. Infect. Immun., 11: 1210-1215.
    • (1975) Infect. Immun. , vol.11 , pp. 1210-1215
    • Gothefors, L.1    Marklund, S.2
  • 16
    • 16644383093 scopus 로고    scopus 로고
    • In vitro and in vivo effects of dantrolene on carbonic anhydrase enzyme activities
    • Gulcin, I, S. Beydemir and M.E. Buyukokuroglu, 2004. In vitro and in vivo effects of dantrolene on carbonic anhydrase enzyme activities. Biol. Pharm. Bull., 27: 613-616.
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 613-616
    • Gulcin, I.1    Beydemir, S.2    Buyukokuroglu, M.E.3
  • 17
    • 0242418224 scopus 로고    scopus 로고
    • Susceptibilities of different Actinobacillus actinomycetemcomitans strains to lactoperoxidase-iodide-hydrogen peroxide combination and different antibiotics
    • Ihalin, R., K. Pienihakkinen, M. Lenander, J. Tenovuo and H. Jousimies-Somer, 2003. Susceptibilities of different Actinobacillus actinomycetemcomitans strains to lactoperoxidase-iodide-hydrogen peroxide combination and different antibiotics. Int. J. Antimicrob. Agents, 21: 434-440.
    • (2003) Int. J. Antimicrob. Agents. , vol.21 , pp. 434-440
    • Ihalin, R.1    Pienihakkinen, K.2    Lenander, M.3    Tenovuo, J.4    Jousimies-Somer, H.5
  • 18
    • 0020639108 scopus 로고
    • Ceftriaxone distribution between maternal blood and fetal blood and tissues at parturition and between blood and milk postpartum
    • Kafetzis, D.A., C. Brater, J.E. Fanourgakis, J. Voyatzis and P. Georgakopoulos, 1983. Ceftriaxone distribution between maternal blood and fetal blood and tissues at parturition and between blood and milk postpartum. Antimicrob. Agents. Chemothr., 23: 870-873.
    • (1983) Antimicrob. Agents. Chemothr. , vol.23 , pp. 870-873
    • Kafetzis, D.A.1    Brater, C.2    Fanourgakis, J.E.3    Voyatzis, J.4    Georgakopoulos, P.5
  • 19
    • 0014949207 scopus 로고
    • Clevage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., 1970. Clevage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0037901694 scopus 로고    scopus 로고
    • Nutritional and physiologic significance of human milk proteins
    • Lonnerdal, B. and E.L. Lien, 2003. Nutritional and physiologic significance of human milk proteins. Am. J. Clm. Nutr., 77: 1537-1543.
    • (2003) Am. J. Clm. Nutr. , vol.77 , pp. 1537-1543
    • Lonnerdal, B.1    Lien, E.L.2
  • 22
    • 0021190031 scopus 로고
    • Transfer of antibiotics into maternal milk
    • Matsuda, S., 1984. Transfer of antibiotics into maternal milk. Biol. Res. Pregnancy Perinatol., 5: 57-60.
    • (1984) Biol. Res. Pregnancy Perinatol , vol.5 , pp. 57-60
    • Matsuda, S.1
  • 23
    • 27744554624 scopus 로고    scopus 로고
    • Sub-second accumulation and stripping for pico-level monitoring of amikacin sulphate by fast fourier transform cyclic voltammetry at a gold microelectrode in flow-injection systems
    • Norouzi, P., G.R. Nabi Bidhendi, M.R. Ganjali, A. Sepehri and M. Ghorbani, 2005. Sub-second accumulation and stripping for pico-level monitoring of amikacin sulphate by fast fourier transform cyclic voltammetry at a gold microelectrode in flow-injection systems. Mikrochimica Acta, 152: 123-129.
    • (2005) Mikrochimica Acta. , vol.152 , pp. 123-129
    • Norouzi, P.1    Nabi Bidhendi, G.R.2    Ganjali, M.R.3    Sepehri, A.4    Ghorbani, M.5
  • 24
    • 28244479764 scopus 로고    scopus 로고
    • In vitro effects of some anaesthetic drugs on lactoperoxidase enzyme activity
    • Özdemir, H. and M.T. Uguz, 2005. In vitro effects of some anaesthetic drugs on lactoperoxidase enzyme activity. J. Enzym. Inhib. Med. Chem., 20: 491-495.
    • (2005) J. Enzym. Inhib. Med. Chem. , vol.20 , pp. 491-495
    • Özdemir, H.1    Uguz, M.T.2
  • 25
    • 0034971280 scopus 로고    scopus 로고
    • Purification of lactoperoxidase from bovine milk and investigation of the kinetic properties
    • Özdemir, H., I. Aygul and O.I. Kufrevioglu, 2001. Purification of lactoperoxidase from bovine milk and investigation of the kinetic properties. Prepep. Biochem. Biotechnol., 31: 125-134.
    • (2001) Prepep. Biochem. Biotechnol , vol.31 , pp. 125-134
    • Özdemir, H.1    Aygul, I.2    Kufrevioglu, O.I.3
  • 26
    • 0037297707 scopus 로고    scopus 로고
    • Immunosuppressive drug use in pregnancy
    • Petri, M., 2003. Immunosuppressive drug use in pregnancy. Autoimmunity, 36: 51-56.
    • (2003) Autoimmunity. , vol.36 , pp. 51-56
    • Petri, M.1
  • 27
    • 0017409303 scopus 로고
    • Enzyme activity of salivary lactoperoxidase adsorbed to human enamel
    • Pruitt, K.M. and M. Adamson, 1977. Enzyme activity of salivary lactoperoxidase adsorbed to human enamel. Infect. Immun., 17: 112-116.
    • (1977) Infect. Immun. , vol.17 , pp. 112-116
    • Pruitt, K.M.1    Adamson, M.2
  • 28
    • 64049090201 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Inhibition of human erythrocyte isozymes I and II with a series of antioxidant phenols
    • Senturk, M., I. Gulcin, A. Dastan, O.I. Kufrevioglu and C.T. Supuran, 2009. Carbonic anhydrase inhibitors. Inhibition of human erythrocyte isozymes I and II with a series of antioxidant phenols. Bioorg. Med. Chem., 17: 3207-3211.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 3207-3211
    • Senturk, M.1    Gulcin, I.2    Dastan, A.3    Kufrevioglu, O.I.4    Supuran, C.T.5
  • 29
    • 0016830865 scopus 로고
    • Steady-state kinetics of lactoperoxidase with ABTS as chromogen
    • Shmdler, J.S. and W.G. Bardsley, 1975. Steady-state kinetics of lactoperoxidase with ABTS as chromogen. Biochem. Biophys. Res. Commun., 67: 1307-1312.
    • (1975) Biochem. Biophys. Res. Commun. , vol.67 , pp. 1307-1312
    • Shmdler, J.S.1    Bardsley, W.G.2
  • 33
    • 3142764923 scopus 로고    scopus 로고
    • Expression and characterization of bovine lactoperoxidase by recombinant baculovirus
    • Tanaka, T., S. Sato, H. Kumura and K. Shimazaki, 2003. Expression and characterization of bovine lactoperoxidase by recombinant baculovirus. Biosci. Biotechnol. Biochem., 67: 2254-2261.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 2254-2261
    • Tanaka, T.1    Sato, S.2    Kumura, H.3    Shimazaki, K.4
  • 34
    • 23644457331 scopus 로고    scopus 로고
    • Purification of bovine milk lactoperoxidase and investigation of antibacterial properties at different thiocyanate mediated
    • Uguz, M.T. and H. Özdemir, 2005. Purification of bovine milk lactoperoxidase and investigation of antibacterial properties at different thiocyanate mediated. Applied Biochem. Microbol., 41: 349-353.
    • (2005) Applied Biochem. Microbol. , vol.41 , pp. 349-353
    • Uguz, M.T.1    Özdemir, H.2
  • 35
    • 44949202618 scopus 로고    scopus 로고
    • The antimicrobial activity of donkey milk and its microflora changes during storage
    • Zhang, X.Y., L. Zhao, L. Jiang, M.L. Dong and F.Z. Ren, 2008. The antimicrobial activity of donkey milk and its microflora changes during storage. Food Control, 19: 1191-1195.
    • (2008) Food Control. , vol.19 , pp. 1191-1195
    • Zhang, X.Y.1    Zhao, L.2    Jiang, L.3    Dong, M.L.4    Ren, F.Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.