1H nuclear magnetic resonance assay of erythrocyte triosephosphate isomerase
A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed. NMR spectroscopy allows the simultaneous monitoring of the substrate and the product of the reaction by virtue of the differences in the NMR spectrum of each chemical species....
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| Published in | Analytical biochemistry Vol. 197; no. 1; pp. 178 - 181 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
San Diego, CA
Elsevier Inc
15.08.1991
Elsevier |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0003-2697 1096-0309 |
| DOI | 10.1016/0003-2697(91)90375-4 |
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| Abstract | A direct method for measuring the activity of erythrocyte triosephosphate isomerase using
1H NMR spectroscopy was developed. NMR spectroscopy allows the simultaneous monitoring of the substrate and the product of the reaction by virtue of the differences in the NMR spectrum of each chemical species. The assay conditions were based on a modification of a conventional spectrophotometric method. The enzymatic activity measured using NMR gave results comparable to those obtained in a standard assay. The results were used in the kinetic characterization of triosephosphate isomerase in hemolysates from subjects with homozygous or heterozygous deficiency of the enzyme. In general, NMR spectroscopy has the potential for wide application in the rapid development of new enzyme assays. |
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| AbstractList | A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed. NMR spectroscopy allows the simultaneous monitoring of the substrate and the product of the reaction by virtue of the differences in the NMR spectrum of each chemical species. The assay conditions were based on a modification of a conventional spectrophotometric method. The enzymatic activity measured using NMR gave results comparable to those obtained in a standard assay. The results were used in the kinetic characterization of triosephosphate isomerase in hemolysates from subjects with homozygous or heterozygous deficiency of the enzyme. In general, NMR spectroscopy has the potential for wide application in the rapid development of new enzyme assays. A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed. NMR spectroscopy allows the simultaneous monitoring of the substrate and the product of the reaction by virtue of the differences in the NMR spectrum of each chemical species. The assay conditions were based on a modification of a conventional spectrophotometric method. The enzymatic activity measured using NMR gave results comparable to those obtained in a standard assay. The results were used in the kinetic characterization of triosephosphate isomerase in hemolysates from subjects with homozygous or heterozygous deficiency of the enzyme. In general, NMR spectroscopy has the potential for wide application in the rapid development of new enzyme assays. A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed. NMR spectroscopy allows the simultaneous monitoring of the substrate and the product of the reaction by virtue of the differences in the NMR spectrum of each chemical species. The assay conditions were based on a modification of a conventional spectrophotometric method. The enzymatic activity measured using NMR gave results comparable to those obtained in a standard assay. The results were used in the kinetic characterization of triosephosphate isomerase in hemolysates from subjects with homozygous or heterozygous deficiency of the enzyme. In general, NMR spectroscopy has the potential for wide application in the rapid development of new enzyme assays.A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed. NMR spectroscopy allows the simultaneous monitoring of the substrate and the product of the reaction by virtue of the differences in the NMR spectrum of each chemical species. The assay conditions were based on a modification of a conventional spectrophotometric method. The enzymatic activity measured using NMR gave results comparable to those obtained in a standard assay. The results were used in the kinetic characterization of triosephosphate isomerase in hemolysates from subjects with homozygous or heterozygous deficiency of the enzyme. In general, NMR spectroscopy has the potential for wide application in the rapid development of new enzyme assays. |
| Author | Hyslop, Serena J. Beal, Patricia Kuchel, Philip W. |
| Author_xml | – sequence: 1 givenname: Serena J. surname: Hyslop fullname: Hyslop, Serena J. organization: Department of Biochemistry, University of Sydney, New South Wales 2006, Australia – sequence: 2 givenname: Patricia surname: Beal fullname: Beal, Patricia organization: The Royal Alexandra Hospital for Children, Camperdown, Sydney, New South Wales 2050, Australia – sequence: 3 givenname: Philip W. surname: Kuchel fullname: Kuchel, Philip W. organization: Department of Biochemistry, University of Sydney, New South Wales 2006, Australia |
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| Cites_doi | 10.1042/bj1140019 10.1002/ana.410170504 10.1016/0002-9343(66)90004-0 10.1056/NEJM196502042720503 10.1016/0009-8981(61)90145-0 10.1182/blood.V64.3.583.583 10.1016/S0021-9258(19)44720-0 10.1021/bi00814a010 |
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| Keywords | Human Proteins Enzymatic activity Enzyme Triosephosphate isomerase Red blood cell NMR spectrometry |
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| References | Beutler (BIB1) 1984 Valentine, Schneider, Baughan, Paglia, Heins (BIB7) 1966; 41 Schneider, Valentine, Baughan, Paglia, Shore, Heins (BIB4) 1968 Bubb, Kirk, Kuchel (BIB11) 1988; 77 Angelman, Brain, MacIver (BIB8) 1970 Van Kampen, Zijlstra (BIB10) 1961; 6 Trentham, McMurray, Pogson (BIB15) 1969; 114 Van Fraunhofen, Murray (BIB13) 1976 Schneider, Valentine, Hattori, Heins (BIB3) 1965; 272 Valentine, Tanaka, Paglia (BIB9) 1989 Kuchel (BIB2) 1989 Poll-The, Aicardi, Girot, Rosa (BIB6) 1985; 17 Sawyer, Tilley, Gracy (BIB16) 1972; 247 Valentine, Paglia (BIB5) 1984; 64 Levitt, Freeman (BIB12) 1979; 33 Gray, Barker (BIB14) 1970; 9 Van Kampen (10.1016/0003-2697(91)90375-4_BIB10) 1961; 6 Angelman (10.1016/0003-2697(91)90375-4_BIB8) 1970 Kuchel (10.1016/0003-2697(91)90375-4_BIB2) 1989 Schneider (10.1016/0003-2697(91)90375-4_BIB4) 1968 Gray (10.1016/0003-2697(91)90375-4_BIB14) 1970; 9 Levitt (10.1016/0003-2697(91)90375-4_BIB12) 1979; 33 Schneider (10.1016/0003-2697(91)90375-4_BIB3) 1965; 272 Bubb (10.1016/0003-2697(91)90375-4_BIB11) 1988; 77 Poll-The (10.1016/0003-2697(91)90375-4_BIB6) 1985; 17 Trentham (10.1016/0003-2697(91)90375-4_BIB15) 1969; 114 Valentine (10.1016/0003-2697(91)90375-4_BIB9) 1989 Van Fraunhofen (10.1016/0003-2697(91)90375-4_BIB13) 1976 Sawyer (10.1016/0003-2697(91)90375-4_BIB16) 1972; 247 Beutler (10.1016/0003-2697(91)90375-4_BIB1) 1984 Valentine (10.1016/0003-2697(91)90375-4_BIB5) 1984; 64 Valentine (10.1016/0003-2697(91)90375-4_BIB7) 1966; 41 |
| References_xml | – volume: 272 start-page: 229 year: 1965 end-page: 235 ident: BIB3 publication-title: N. Engl. J. Med – volume: 33 start-page: 473 year: 1979 end-page: 476 ident: BIB12 publication-title: J. Magn. Reson – start-page: 157 year: 1989 ident: BIB2 publication-title: Analytical NMR – volume: 247 start-page: 6499 year: 1972 end-page: 6505 ident: BIB16 publication-title: J. Biol. Chem – start-page: 34 year: 1976 ident: BIB13 article-title: Statistics in Medical, Dental and Biological Studies – volume: 9 start-page: 2454 year: 1970 end-page: 2462 ident: BIB14 publication-title: Biochemistry – start-page: 2350 year: 1989 ident: BIB9 publication-title: The Metabolic Basis of Inherited Disease – start-page: 122 year: 1970 ident: BIB8 publication-title: Abstracts, XIIIth International Congress Hematology – year: 1984 ident: BIB1 article-title: Red Cell Metabolism: A Manual of Biochemical Methods – volume: 77 start-page: 363 year: 1988 end-page: 368 ident: BIB11 publication-title: J. Magn. Reson – volume: 64 start-page: 583 year: 1984 end-page: 591 ident: BIB5 publication-title: Blood – volume: 17 start-page: 439 year: 1985 end-page: 443 ident: BIB6 publication-title: Ann. Neurol – start-page: 265 year: 1968 ident: BIB4 publication-title: Hereditary Disorders of Erythrocyte Metabolism – volume: 6 start-page: 538 year: 1961 end-page: 544 ident: BIB10 publication-title: Clin. Chim. Acta – volume: 114 start-page: 19 year: 1969 end-page: 24 ident: BIB15 publication-title: Biochem. J – volume: 41 start-page: 27 year: 1966 end-page: 41 ident: BIB7 publication-title: Am. J. Med – year: 1984 ident: 10.1016/0003-2697(91)90375-4_BIB1 – volume: 114 start-page: 19 year: 1969 ident: 10.1016/0003-2697(91)90375-4_BIB15 publication-title: Biochem. J doi: 10.1042/bj1140019 – volume: 17 start-page: 439 year: 1985 ident: 10.1016/0003-2697(91)90375-4_BIB6 publication-title: Ann. Neurol doi: 10.1002/ana.410170504 – start-page: 157 year: 1989 ident: 10.1016/0003-2697(91)90375-4_BIB2 – volume: 41 start-page: 27 year: 1966 ident: 10.1016/0003-2697(91)90375-4_BIB7 publication-title: Am. J. Med doi: 10.1016/0002-9343(66)90004-0 – start-page: 34 year: 1976 ident: 10.1016/0003-2697(91)90375-4_BIB13 article-title: Statistics in Medical, Dental and Biological Studies – start-page: 122 year: 1970 ident: 10.1016/0003-2697(91)90375-4_BIB8 – volume: 272 start-page: 229 year: 1965 ident: 10.1016/0003-2697(91)90375-4_BIB3 publication-title: N. Engl. J. Med doi: 10.1056/NEJM196502042720503 – volume: 33 start-page: 473 year: 1979 ident: 10.1016/0003-2697(91)90375-4_BIB12 publication-title: J. Magn. Reson – volume: 6 start-page: 538 year: 1961 ident: 10.1016/0003-2697(91)90375-4_BIB10 publication-title: Clin. Chim. Acta doi: 10.1016/0009-8981(61)90145-0 – start-page: 2350 year: 1989 ident: 10.1016/0003-2697(91)90375-4_BIB9 – volume: 64 start-page: 583 year: 1984 ident: 10.1016/0003-2697(91)90375-4_BIB5 publication-title: Blood doi: 10.1182/blood.V64.3.583.583 – volume: 247 start-page: 6499 year: 1972 ident: 10.1016/0003-2697(91)90375-4_BIB16 publication-title: J. Biol. Chem doi: 10.1016/S0021-9258(19)44720-0 – start-page: 265 year: 1968 ident: 10.1016/0003-2697(91)90375-4_BIB4 – volume: 77 start-page: 363 year: 1988 ident: 10.1016/0003-2697(91)90375-4_BIB11 publication-title: J. Magn. Reson – volume: 9 start-page: 2454 year: 1970 ident: 10.1016/0003-2697(91)90375-4_BIB14 publication-title: Biochemistry doi: 10.1021/bi00814a010 |
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| Snippet | A direct method for measuring the activity of erythrocyte triosephosphate isomerase using
1H NMR spectroscopy was developed. NMR spectroscopy allows the... A direct method for measuring the activity of erythrocyte triosephosphate isomerase using 1H NMR spectroscopy was developed. NMR spectroscopy allows the... |
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| SubjectTerms | Analytical, structural and metabolic biochemistry Biological and medical sciences Enzymes and enzyme inhibitors Erythrocytes - enzymology Fundamental and applied biological sciences. Psychology Hemolysis Heterozygote Homozygote Humans Hydrogen Magnetic Resonance Spectroscopy - methods Triose-Phosphate Isomerase - blood Triose-Phosphate Isomerase - deficiency Triose-Phosphate Isomerase - genetics |
| Title | 1H nuclear magnetic resonance assay of erythrocyte triosephosphate isomerase |
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