Zobrazeno 1 - 10
of 14
pro vyhledávání: '"T. W. Esders"'
Autor:
T W Esders, C T Goodhue, B Bruschi, R N Rand, J Figueras, R W Spayd, R W Nelson, Tai-Wing Wu, D D LaRossa, J N Eikenberry, G M Dappen, B A Burdick
Publikováno v:
Clinical Chemistry. 24:1343-1350
Using the general concept of a dry multilayer analytical element, we can change chemical procedures and configurations to assay several blood components. In the assay of serum urea nitrogen, urease in the reagent layer catalyzes the hydrolysis of ure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4d27338f384c2583fe4bd904e0767ad3
https://doi.org/10.1093/clinchem/24.8.1343
https://doi.org/10.1093/clinchem/24.8.1343
Autor:
Robert J. Limhardt, K. L. Carleton, J. P. Rowland, M. J. Daniels, D. M. Farmer, I. Ehrenthal, K. E. Miner, J. T. Johansen, J. Maurukas, G. T. McCollough, T. W. Esders, S. Y. Lynn, I. E. Modrovich, K. Oyama, S. Nishimura, Y. Nonaka, T. Hashimoto, K. Kihara, A. Sakimae, H. Onishi, H. Schutt, L. I. Stekolnikov, B. A. Sevastyanov, G. G. Shilov, A. A. Belousov, N. D. Mamonov
Publikováno v:
Applied Biochemistry and Biotechnology. 12:67-76
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd95ae59cba6b1b954dce10557efe9bc
https://doi.org/10.1007/bf02798579
https://doi.org/10.1007/bf02798579
Publikováno v:
Clinical Chemistry. 29:645-649
We developed a thin-film enzymic assay for creatinine that makes use of creatinine iminohydrolase (EC 3.5.4.21) to convert creatinine to N-methylhydantoin and ammonia. The ammonia diffuses through a semipermeable layer and is quantitated by reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61185f6e7416e4633c0e9c355fb8bc36
https://doi.org/10.1093/clinchem/29.4.645
https://doi.org/10.1093/clinchem/29.4.645
Autor:
S Y Lynn, T W Esders
Publikováno v:
Journal of Biological Chemistry. 260:3915-3922
Creatinine iminohydrolase (EC 3.5.4.21), which catalyzes hydrolysis of creatinine to N-methylhydantoin and ammonia, was purified from Flavobacterium filamentosum. The average molecular weight of the purified enzyme was 272,480, and the subunit molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cdad5430e84212d98478ef7c0cb45e3
https://doi.org/10.1016/s0021-9258(18)89209-2
https://doi.org/10.1016/s0021-9258(18)89209-2
Autor:
C A Michrina, T W Esders
Publikováno v:
Journal of Biological Chemistry. 254:2710-2715
A procedure was developed to purify the Streptococcus faecium ATCC 12755 L-alpha-glycerophosphate oxidase. The molecular weight of the purified enzyme was 131,000 and the subunit molecular weight was 72,000. Two moles of FAD were bound/mol of enzyme.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::015d2f04f36a7443ca43b7e9b70f3913
https://doi.org/10.1016/s0021-9258(17)30130-8
https://doi.org/10.1016/s0021-9258(17)30130-8
Autor:
R W, Spayd, B, Bruschi, B A, Burdick, G M, Dappen, J N, Eikenberry, T W, Esders, J, Figueras, C T, Goodhue, D D, LaRossa, R W, Nelson, R N, Rand, T W, Wu
Publikováno v:
Clinical chemistry. 24(8)
Using the general concept of a dry multilayer analytical element, we can change chemical procedures and configurations to assay several blood components. In the assay of serum urea nitrogen, urease in the reagent layer catalyzes the hydrolysis of ure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4b996b8ff3cfdba5bad6b63c8c781ba4
https://pubmed.ncbi.nlm.nih.gov/567106
https://pubmed.ncbi.nlm.nih.gov/567106
Autor:
T W, Esders, C A, Michrina
Publikováno v:
The Journal of biological chemistry. 254(8)
A procedure was developed to purify the Streptococcus faecium ATCC 12755 L-alpha-glycerophosphate oxidase. The molecular weight of the purified enzyme was 131,000 and the subunit molecular weight was 72,000. Two moles of FAD were bound/mol of enzyme.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c8919b06ab92068efc280a892054129e
https://pubmed.ncbi.nlm.nih.gov/429313
https://pubmed.ncbi.nlm.nih.gov/429313
Autor:
T W, Esders, S Y, Lynn
Publikováno v:
The Journal of biological chemistry. 260(7)
Creatinine iminohydrolase (EC 3.5.4.21), which catalyzes hydrolysis of creatinine to N-methylhydantoin and ammonia, was purified from Flavobacterium filamentosum. The average molecular weight of the purified enzyme was 272,480, and the subunit molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e80104ce4d0356016441758aa7751766
https://pubmed.ncbi.nlm.nih.gov/3980459
https://pubmed.ncbi.nlm.nih.gov/3980459
Publikováno v:
Clinical chemistry. 29(4)
We developed a thin-film enzymic assay for creatinine that makes use of creatinine iminohydrolase (EC 3.5.4.21) to convert creatinine to N-methylhydantoin and ammonia. The ammonia diffuses through a semipermeable layer and is quantitated by reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a4bafb917da10126aac5d2f6a118bf8e
https://pubmed.ncbi.nlm.nih.gov/6831692
https://pubmed.ncbi.nlm.nih.gov/6831692
Autor:
T W, Esders, R J, Light
Publikováno v:
The Journal of biological chemistry. 247(5)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8eb1944004c410460cbf4a1205c68435
https://pubmed.ncbi.nlm.nih.gov/5012313
https://pubmed.ncbi.nlm.nih.gov/5012313