Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Bovine kidney

Kucera j, Mader P, Miholova D, Cibulka J, Faltejsek J and Kordik D (1995) Preparation of the bovine kidney and bovine muscle reference materials and the certification of element contents fi om interlaboratory comparisons. Fresenius J Anal Chem 352 66-72. [Pg.17]

Storage stability studies for carfentrazone-ethyl compounds on crop matrices have shown a pattern of stability for at least 7-24 months, depending on the study program or the maximum sample storage interval for the study. Carfentrazone-ethyl was not stable in field corn starch, potato tuber and bovine kidney. The residue results indicated that a significant portion of carfentrazone-ethyl was converted to C-Cl-PAc in these matrices however, the total amount of carfentrazone-ethyl and C-Cl-PAc accounted for the original spiking level. Since both carfentrazone-ethyl and C-Cl-PAc were determined in these stability studies, the instability of carfentrazone-ethyl was not of any concern. [Pg.488]

Fig. 14.3. Stoichiometry of phosphorylation/inactivation of the bovine kidney and A. suum E1 isoforms. Adult A. suum PDC was depleted of its E1 component and reconstituted with either bovine kidney E1 or recombinant A. suum E1s containing either the al or all isoform (Klingbeil etal., 1997 Huang etal., 1998b). The hybrid complexes were then assayed for PDC activity and the incorporation of 32P, as described fully in Thissen etal. (1986). Upper panel o, bovine kidney E1 , E1 isolated directly from the adult A. suum PDC. Lower panel , A. suum E1al isoform , A. suum E1all isoform. Fig. 14.3. Stoichiometry of phosphorylation/inactivation of the bovine kidney and A. suum E1 isoforms. Adult A. suum PDC was depleted of its E1 component and reconstituted with either bovine kidney E1 or recombinant A. suum E1s containing either the al or all isoform (Klingbeil etal., 1997 Huang etal., 1998b). The hybrid complexes were then assayed for PDC activity and the incorporation of 32P, as described fully in Thissen etal. (1986). Upper panel o, bovine kidney E1 , E1 isolated directly from the adult A. suum PDC. Lower panel , A. suum E1al isoform , A. suum E1all isoform.
Rahmatullah, M. and Roche, T.E. (1985) Modification of bovine kidney pyruvate dehydrogenase kinase activity by CoA esters and their mechanism of action. Journal of Biological Chemistry 260, 10146—10152. [Pg.290]

The guanidino analogue 90 of the 7-membered cyclic urea system was prepared, enantiomerically pure, from D-mannitol. The derivative 90 selectively inhibits bovine kidney a-L-fucosidase at 2.8pM <00BMC307>. [Pg.358]

Vandenbroeck et al.7 used an ELISA to determine the recovery of immu-noreactive porcine interferon-gamma (IFN-y) from E. coli inclusion bodies. The ELISA used a polyclonal coating antibody with detection by a MAb. The inclusion bodies were solubilized in diluted 6 M guanidine/HCl and IFN subsequently refolded by its removal. The antiviral activity of the interferon was measured with a bioassay using the cytopathic effect (CPE) of vesicular stomatitis virus (VSV) on bovine kidney cells. The results of this study showed that the immu-noreactivity measured by ELISA matched the biological activity measured by bioassay. [Pg.286]

An amidrazone (58) derived from 5-amino-5-deoxy-L-fuconolactam was found to inhibit a recombinant human a-L-fucosidase with a K -value of 820 nmol/1 [ 111 ]. A simple synthesis of 1,5-dideoxy-1,5-imino-D-arabinitol (59), previously prepared by Ganem et al. [49] as a potential maimosidase inhibitor, was applied to the affinity purification of a-L-fucosidase from bovine kidney by an improved method and the characterization of the enzyme thus obtained [112]. The relatively low affinity of this compound to the enzyme (Kj 2.2 pmol/1 at pH 7) compared to 1-deoxyfuconoJirimycin (51) turned out to be advantageous in terms of enzyme recovery and yield. Structurally related, suitably protected 5-amino-5-deoxy-D-arabinopyranose (60), was coupled with a N-acetyl-6-deoxy-6-thio-D-glucosaminide (61) to give a stable thioglycoside (62) [113]. [Pg.172]

Interestingly, erythrocytes that had lost (2—>3)-sialyl residues were still agglutinable by influenza viruses.531 In similar experiments with Madin-Darby, bovine kidney-cells and Sendai viruses, (2— 3)-sialyl residues as components of the oligosaccharide sequence a-Neu5Ac-(2— 3)-/3-Gal-(T 3)-GalNAc constitute specific receptors for these... [Pg.229]

Lawson, R. Cook, K.G. Yeaman, S.J. Rapid purification of bovine kidney branched-chain 2-oxoacid dehydrogenase complex containing endogenous kinase activity. FEBS Lett., 157, 54-58 (1982)... [Pg.25]

Lee, H.Y. Hall, T.B. Kee, S.M. Tung, H.Y.L. Reed, L.J. Purification and properties of branched-chain a-keto acid dehydrogenase kinase from bovine kidney. BioFactors, 3, 109-112 (1991)... [Pg.26]

Imidocarb Bovine kidney Bond-Elut CBA MeOH MeOH contg TEA 316... [Pg.594]

Fig. 29.1 HPLC-PDA of (a) MSPD extract of control bovine kidney, (b) MSPD extract of bovine kidney fortified at the 20 ppm level, and (c) synthetic mixture of standards at levels of 15 ng per component injected. Peaks 1, spectinomycin 2, hygromycin B 3, streptomycin 4, dihydrostreptomycin. (Reprinted from Ref. 19 with permission from Elsevier Science.)... Fig. 29.1 HPLC-PDA of (a) MSPD extract of control bovine kidney, (b) MSPD extract of bovine kidney fortified at the 20 ppm level, and (c) synthetic mixture of standards at levels of 15 ng per component injected. Peaks 1, spectinomycin 2, hygromycin B 3, streptomycin 4, dihydrostreptomycin. (Reprinted from Ref. 19 with permission from Elsevier Science.)...
When bovine-comeal, peptido-keratan sulfate was degraded chemically, a tetrasaccharide fraction was obtained, and the sequence in this was determined from the hydrolytic pattern with E. coli jS-D-galactosidase, Canavalia ensiformis a-D-mannosidase (EC 3.2.1.24), human-placental / -D-mannosidase, and bovine-kidney a-L-fucosidase. 72... [Pg.209]

Mutarotation of 0.3% solutions of the freshly dissolved sugars in 12 ml of 5 mM EDTA, pH 7.4 was followed. Significant differences in mutarotation rates (AK) in the presence and absence of 100 units of bovine kidney enzyme were expressed as the ratio AK/Ksp. Differences of less than 5% in these rate constants were not considered significant. Of the 18 sugars listed, nine have been tested previously as substrates for other mammalian mutarotases with essentially the same pattern as described here. The pattern of specificity indicates that a 3-point attachment of enzyme and substrate is necessary for catalysis of mutarotation. b Data from 72). [Pg.286]

Figure 5. Competitive inhibitors of bovine kidney mutarotase... Figure 5. Competitive inhibitors of bovine kidney mutarotase...
Isolation and Characterisation of a Mutarotase from Bovine Kidney Cortex, J. Biol. Chem. (1969) 244, 781. [Pg.314]

The vitamin D activity in animal products is contributed by both vitamin D3 and 25-hy-droxyvitamin D3. Typical values of the hydroxylated metabolite (/zg/100 g) are bovine muscle, 0.2-0.3 bovine liver, 0.3-0.5 bovine kidney, 0.5-1.0 (36) and egg yolk, 1.0 (37). 25-Hydrox-yvitamin D3 is of nutritional significance it is about five times more potent than vitamin D3 and occurs in significant amounts. In milk, for example, it accounts for 75% of the total vitamin D activity as estimated by the calcium transport assay (38). [Pg.331]

An electrospray ionization LC-MS-MS assay was developed for the determination of OTC, TC, CTC, and DXC in bovine liver and muscle. The TCs gave three fragmentation ions in the electrospray mass spectra, except for DXC, and these ions are very useful for confirmation. In order to obtain optimal tandem MS conditions, the mass spectra were measured at different collision offsets, and the intensity of ions were measured. This method could confirm TCs below the lOO-yttg/kg level in the bovine kidney and muscle (44). [Pg.630]

Van Eeckhout, N., Perez, J. C., and Van Peteghem, C. (2000). Determination of eight sulfonamides in bovine kidney by liquid chromatography/tandem mass spectrometry with on-line extraction and sample clean-up. Rapid Commun. Mass Spectrom. 14 2331-2338. [Pg.339]

Puro, K. Isolation of bovine kidney gangliosides. Acta Chem. Scan., 1970, 24(1), 13-22. [Pg.13]


See other pages where Bovine kidney is mentioned: [Pg.18]    [Pg.337]    [Pg.488]    [Pg.167]    [Pg.284]    [Pg.291]    [Pg.109]    [Pg.100]    [Pg.162]    [Pg.221]    [Pg.112]    [Pg.171]    [Pg.31]    [Pg.441]    [Pg.433]    [Pg.592]    [Pg.604]    [Pg.888]    [Pg.604]    [Pg.112]    [Pg.171]    [Pg.287]    [Pg.299]    [Pg.301]    [Pg.302]    [Pg.303]    [Pg.319]    [Pg.23]    [Pg.24]   
See also in sourсe #XX -- [ Pg.393 ]

See also in sourсe #XX -- [ Pg.393 ]




SEARCH



© 2024 chempedia.info