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Volumn 331, Issue 1, 2004, Pages 115-121

The use of Fourier transform infrared spectroscopy to assay for urease from Pseudomonas aeruginosa and Canavalia ensiformis

Author keywords

Enzyme activity; Fourier Transform Infrared Spectroscopy (FTIR); Hydrolysis; Urea; Urease from Pseudomonas aeruginosa and Canavalia ensiformis

Indexed keywords

AMIDES; BACTERIA; ENZYME ACTIVITY; HEAVY WATER; HYDROLYSIS; KINETICS; METABOLISM; SPECTROPHOTOMETRY; SPECTROSCOPIC ANALYSIS; UREA;

EID: 3042794573     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(04)00360-4     Document Type: Article
Times cited : (29)

References (22)
  • 2
    • 0034116225 scopus 로고    scopus 로고
    • Rapid urease tests lack sensitivity in Helicobacter pylori diagnosis when peptic ulcer disease presents with bleeding
    • Lee J.M., Breslin N.P., Fallon C., O'Morain C.A. Rapid urease tests lack sensitivity in Helicobacter pylori diagnosis when peptic ulcer disease presents with bleeding. Am. J. Gastroenterol. 95:2000;1166-1170
    • (2000) Am. J. Gastroenterol. , vol.95 , pp. 1166-1170
    • Lee, J.M.1    Breslin, N.P.2    Fallon, C.3    O'Morain, C.A.4
  • 3
    • 0034585129 scopus 로고    scopus 로고
    • Plant ureases: Role and regulation
    • Sirko A., Brodzik R. Plant ureases: role and regulation. Acta Biochim. Polonica. 47:2000;1189-1195
    • (2000) Acta Biochim. Polonica , vol.47 , pp. 1189-1195
    • Sirko, A.1    Brodzik, R.2
  • 4
    • 33947332625 scopus 로고
    • Phenol-hypochlorite reaction for determination of ammonia
    • Weatherburn M.W. Phenol-hypochlorite reaction for determination of ammonia. Anal. Chem. 39:1967;971-974
    • (1967) Anal. Chem. , vol.39 , pp. 971-974
    • Weatherburn, M.W.1
  • 5
    • 0013925072 scopus 로고
    • NADH-dependent coupled enzyme assay for urease and other ammonia-producing systems
    • Kaltwasser H., Schlegel H.G. NADH-dependent coupled enzyme assay for urease and other ammonia-producing systems. Anal. Biochem. 16:1966;132-138
    • (1966) Anal. Biochem. , vol.16 , pp. 132-138
    • Kaltwasser, H.1    Schlegel, H.G.2
  • 6
    • 0015530488 scopus 로고
    • Urease: A sensitive and specific radiometric assay
    • McDonald J.A., Speeg K.V., Campbell J.W. Urease: a sensitive and specific radiometric assay. Enzymologia. 42:1972;1-9
    • (1972) Enzymologia , vol.42 , pp. 1-9
    • McDonald, J.A.1    Speeg, K.V.2    Campbell, J.W.3
  • 7
    • 0034948186 scopus 로고    scopus 로고
    • Strategies in the preparation of DNA oligonucleotide arrays for diagnostic applications
    • Beaucage S.L. Strategies in the preparation of DNA oligonucleotide arrays for diagnostic applications. Curr. Med. Chem. 8:2001;1213-1244
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1213-1244
    • Beaucage, S.L.1
  • 8
    • 0035916253 scopus 로고    scopus 로고
    • Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms
    • Zscherp C., Barth A. Reaction-induced infrared difference spectroscopy for the study of protein reaction mechanisms. Biochemistry. 40:2001;1875-1883
    • (2001) Biochemistry , vol.40 , pp. 1875-1883
    • Zscherp, C.1    Barth, A.2
  • 9
    • 0034452798 scopus 로고    scopus 로고
    • Infrared spectroscopy in solid-phase synthesis
    • De Miguel Y.R., Shearer A.S. Infrared spectroscopy in solid-phase synthesis. Biotechnol. Bioeng. 71:2001;119-129
    • (2001) Biotechnol. Bioeng. , vol.71 , pp. 119-129
    • De Miguel, Y.R.1    Shearer, A.S.2
  • 10
    • 0031423671 scopus 로고    scopus 로고
    • Infrared spectroscopy: A new frontier in medicine
    • Jackson M., Sowa M.G., Petersen H.H. Infrared spectroscopy: a new frontier in medicine. Biophys. Chem. 68:1999;109-125
    • (1999) Biophys. Chem. , vol.68 , pp. 109-125
    • Jackson, M.1    Sowa, M.G.2    Petersen, H.H.3
  • 11
    • 0036670581 scopus 로고    scopus 로고
    • Direct measurement of enzyme activity with infrared spectroscopy
    • Thoenges D., Barth A. Direct measurement of enzyme activity with infrared spectroscopy. J. Biomol. Screen. 7:2002;353-357
    • (2002) J. Biomol. Screen. , vol.7 , pp. 353-357
    • Thoenges, D.1    Barth, A.2
  • 12
    • 0142257962 scopus 로고    scopus 로고
    • A FTIR spectroscopic based method for measuring enzymatic activity of a recombinant amidase
    • Pacheco R., Serralheiro M.L.M., Karmali A., Haris P.I. A FTIR spectroscopic based method for measuring enzymatic activity of a recombinant amidase. Anal. Biochem. 322:2003;208-214
    • (2003) Anal. Biochem. , vol.322 , pp. 208-214
    • Pacheco, R.1    Serralheiro, M.L.M.2    Karmali, A.3    Haris, P.I.4
  • 13
    • 0000527093 scopus 로고
    • Induction and repression of Pseudomonas aeruginosa amidase
    • Brammar W.J., Clark P.H. Induction and repression of Pseudomonas aeruginosa amidase. J. Gen. Microbiol. 37:1964;307-319
    • (1964) J. Gen. Microbiol. , vol.37 , pp. 307-319
    • Brammar, W.J.1    Clark, P.H.2
  • 14
    • 0017743354 scopus 로고
    • Pseudomonas aeruginosa mutants resistant to urea inhibition of growth on acetanilide
    • Gregoriou M., Brown P.R., Tata R. Pseudomonas aeruginosa mutants resistant to urea inhibition of growth on acetanilide. J. Bacteriol. 132:1977;377-384
    • (1977) J. Bacteriol. , vol.132 , pp. 377-384
    • Gregoriou, M.1    Brown, P.R.2    Tata, R.3
  • 15
    • 0034966202 scopus 로고    scopus 로고
    • Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability
    • Karmali A., Pacheco R., Tata R., Brown P.R. Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability. Mol. Biotechnol. 17:2001;200-212
    • (2001) Mol. Biotechnol. , vol.17 , pp. 200-212
    • Karmali, A.1    Pacheco, R.2    Tata, R.3    Brown, P.R.4
  • 16
    • 85168631491 scopus 로고
    • One-step affinity purification of urease from Jack Beans
    • Mendes M.J., Karmali A., Brown P.R. One-step affinity purification of urease from Jack Beans. Biochimie. 70:1988;1369-1371
    • (1988) Biochimie , vol.70 , pp. 1369-1371
    • Mendes, M.J.1    Karmali, A.2    Brown, P.R.3
  • 17
    • 0031708121 scopus 로고    scopus 로고
    • One-step purification of urease from Canavalia ensiformis by immobilized metal affinity chromatography
    • Sousa C., Karmali A. One-step purification of urease from Canavalia ensiformis by immobilized metal affinity chromatography. Int. J. Biochromatogr. 4:1998;15-25
    • (1998) Int. J. Biochromatogr. , vol.4 , pp. 15-25
    • Sousa, C.1    Karmali, A.2
  • 18
    • 0001245278 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 101:1976;200-203
    • (1976) Anal. Biochem. , vol.101 , pp. 200-203
    • Bradford, M.M.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.). 227:1970;680-685
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0001232852 scopus 로고
    • An Introduction of Polyacrylamide Gel Electrophoresis
    • B.D. Hames, & Rickwood. Oxford: IRL Press
    • Hames B.D. An Introduction of Polyacrylamide Gel Electrophoresis. Hames B.D., Rickwood Gel Electrophoresis of Proteins. 1981;1-86 IRL Press, Oxford
    • (1981) Gel Electrophoresis of Proteins , pp. 1-86
    • Hames, B.D.1
  • 21
    • 0018900433 scopus 로고
    • An improved method for detection and preservation of urease activity in polyacrylamide gel
    • Shaik-M M.B., Guy A.L., Pancholy S.K. An improved method for detection and preservation of urease activity in polyacrylamide gel. Anal. Biochem. 103:1980;140-143
    • (1980) Anal. Biochem. , vol.103 , pp. 140-143
    • Shaik-M, M.B.1    Guy, A.L.2    Pancholy, S.K.3
  • 22
    • 0014669553 scopus 로고
    • Urease catalysis - Stoichiometry, kinetics and inhibitory properties of a third substrate: Dihydroxyurea
    • Fishbein W.N. Urease catalysis - stoichiometry, kinetics and inhibitory properties of a third substrate: dihydroxyurea. J. Biol. Chem. 244:1969;1188-1193
    • (1969) J. Biol. Chem. , vol.244 , pp. 1188-1193
    • Fishbein, W.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.