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Monovalent cation activation of tryptophanase

Autor: E E Snell, C H Suelter

Publikováno v: Journal of Biological Chemistry. 252:1852-1857

The interaction of monovalent cations with holotryptophanase has been examined by spectral and kinetic methods. Using S-orthonitrophenyl-L-cysteine as a substrate, activation by the following monovalent cations was demonstrated; values of KA (mM, in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3cd0cab80185c3c611c21236834742ee
https://doi.org/10.1016/s0021-9258(18)71835-8

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Human erythrocyte 5'-AMP aminohydrolase. Purification and characterization

Autor: C H Suelter, S Yun

Publikováno v: Journal of Biological Chemistry. 253:404-408

Human erythrocyte 5'-AMP aminohydrolase has been obtained using phosphocellulose chromatography and affinity chromatography on a GTP-agarose column to yield a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme has a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::814d1cee7a1b59c5df1eca3d5e627522
https://doi.org/10.1016/s0021-9258(17)38223-6

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Homogeneous pyruvate kinase isolated from yeast by two different methods is indistinguishable from pyruvate kinase in cell-free extract

Autor: A E Aust, C H Suelter

Publikováno v: Journal of Biological Chemistry. 253:7508-7512

In this report, we have compared homogeneous yeast (Saccharomyces cerevisiae) pyruvate kinase to enzyme from cell-free extracts in several different ways: 1) isoelectric focusing of cell-free extracts indicates one peak of pyruvate kinase activity wh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cd059b6f34288b8fb121c9d8d7504f69
https://doi.org/10.1016/s0021-9258(17)34532-5

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Circulatory clearance, internalization, and degradation of muscle AMP aminohydrolase

Autor: C H Suelter, H D Husic

Publikováno v: Journal of Biological Chemistry. 259:4359-4364

Chicken muscle AMP aminohydrolase is cleared rapidly from the circulation of chickens after intravenous injection of the purified enzyme (Husic, H. D., and Suelter, C. H. (1980) Biochem. Biophys. Res. Commun. 95, 228-235). After the intravenous injec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c5de04ee13cf398047b3f30e85c3c5bb
https://doi.org/10.1016/s0021-9258(17)43054-7

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Quantitation of the efflux of acylcarnitines from rat heart, brain, and liver mitochondria

Autor: Loran L. Bieber, W Lysiak, P P Toth, C H Suelter

Publikováno v: Journal of Biological Chemistry. 261:13698-13703

The efflux of individual short-chain and medium-chain acylcarnitines from rat liver, heart, and brain mitochondria metabolizing several substrates has been measured. The acylcarnitine efflux profiles depend on the substrate, the source of mitochondri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4153bf37f95cc0cd2ae08dfd90a4916a
https://doi.org/10.1016/s0021-9258(18)67077-2

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Principal component analysis of rapid scanning wavelength stopped-flow kinetics experiments on the liver alcohol dehydrogenase catalyzed reduction of p-nitroso-N,N-dimethylaniline by 1,4-dihydronicotinamide adenine dinucleotide

Autor: J. Ceraso, James L. Dye, F. H. Horne, C. H. Suelter, R. N. Cochran

Publikováno v: The Journal of Physical Chemistry. 84:2567-2575

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::82652651deda961b5417c92a7ae09700
https://doi.org/10.1021/j100457a017

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Binding, internalization, and degradation of AMP aminohydrolase by avian hepatocyte monolayers

Autor: C H Suelter, H D Husic

Publikováno v: Journal of Biological Chemistry. 259:4365-4371

Chicken muscle AMP aminohydrolase is cleared from the circulation of chickens after intravenous injection of the purified enzyme with a half-life of 3-5 min (Husic, H.D., and Suelter, C.H. (1980) Biochem. Biophys. Res. Commun. 95, 228-235). The enzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bda76703897f285e3afb960b7170d452
https://doi.org/10.1016/s0021-9258(17)43055-9

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