Serum rabbit

MCPBA converts the MTM ester to a methylsulfonylmethyl ester (78-98% yield), which can be hydrolyzed enzymatically with rabbit serum (pH 4.5 phosphate buffer, EtOH, 25-28°, 1 h, 84% yield). ... [Pg.389]

Peptides formed during tryptic digest of Salmonella flagellin were immobilized on the WPG-PG to prepare immunoadsorbents for the isolation of monoreceptor antibodies from rabbit serum against H-antigens of Salmonella spp. [129]. The... [Pg.171]

Monkos, Karol 2005. A comparison of solution conformation and hydrodynamic properties of equine, porcine and rabbit serum albumin using viscometric measurements. Biochimica et Biophysica Acta 1748,100-109. [Pg.114]

NPY Neuropeptide Y NRS Normal rabbit serum NSAID Non-steroidal antiinflammatory drug NSE Nerve-specific enolase NT Neurotensin N terminus Amino terminus of peptide... [Pg.285]

Stainless steel column (25 cm x 4.6 mm) of YWG-C18H37 (10 pm) Aqueous 85% methanol [1.5 mL/min] 267 nm Reversed-phase HPLC analysis in rabbit serum. [97]... [Pg.193]

The utility of a process control was demonstrated by constructing a series of slides containing mouse and rabbit serum. Five rows of a series of dilutions of each species were applied to slides, and these were then stained in mixed cocktails of goat anti-rabbit and goat anti-mouse secondary antibody, followed by routine peroxidase-DAB visualization steps. The mixed cocktails were constructed as variable mixtures to demonstrate the ability to detect lack of sensitivity of either of the cocktail components. The results of this study were published in abstract form.15 Clearly, this approach can provide a way to monitor changes in secondary antibody cocktails, either due to manufacturing variables or differential aging of components within the cocktail (Fig. 10.5). [Pg.180]

Figure 10.5 A series of slides printed with dilutions of mouse serum and rabbit serum. There are five replicates of each species, and all slides have identical printing. The secondary antibody cocktail was constructed according to the labels on each slide. This demonstrates that a control slide can easily detect sensitivity changes in secondary antibodies.

The most common carrier proteins in use today are keyhole limpet hemocyanin (KLH MW 4.5 X 105 to 1.3 X 107), BSA (MW 67,000), aminoethylated (or cationized) BSA (cBSA), thyroglobulin (MW 660,000), ovalbumin (OVA MW 43,000), and various toxoid proteins, including tetanus toxoid and diphtheria toxoid. Other proteins occasionally used include myoglobin, rabbit serum albumin, immunoglobulin molecules (particularly IgG) from bovine or mouse sera, tuberculin purified protein derivative, and synthetic polypeptides such as poly-L-lysine and poly-L-glutamic acid. [Pg.748]

Number of Treatment Rabbits Serum Lipids (mg/dl) Atherosclerosis Cholesterol Triglycerides Arch Thoracic ... [Pg.156]

It has been observed that while normal, rabbit serum failed to bind labelled phenobarbital, the serum from immunized rabbits bound 75 to 80% of the added pentobarbital and there exists a linear relationship between 14C-phenobarbital and the concentration of added antibody. Besides, when variable quantities of 14C-pentobarbital are added to a constant quantity of antibody, there exists a linear relationship between added and bound 14C-phenobarbital as depicted in Figure 32.4. [Pg.500]

Figure 6.1. Fluorescence polarization immunoassay for theophylline. (A) Effect of theophylline rabbit antiserum ( ) and normal rabbit serum (A) on the fluorescence polarization of the theophylline-umbelliferone conjugate. (B) Fluorescence polarization of the theophylline-umbelliferone conjugate in the presence of varying concentrations of theophylline. (Reprinted from Ref. 1, with permission from Academic Press.)...

C. L. Kuo, B. N. La Du, Comparison of Purified Human and Rabbit Serum Paraoxonases , Drug Metab. Dispos. 1995, 23, 935-944 C. L. Kuo, B. N. La Du, Calcium Binding by Human and Rabbit Serum Paraoxonases. Structural Stability and Enzymatic Activity , Drug Metab. Dispos. 1998, 26, 653-660. [Pg.95]

Phosphinates are a class of organophosphorus compounds, the metabolism of which has received less attention than that of phosphates (see above) or phosphorothioates and P-halidc compounds (see below). Many phosphinates are rapid but transient inhibitors of acetylcholinesterase and carboxyl-esterases. And like organophosphates and phosphonates, phosphinates are substrates of arylesterases (EC 3.1.1.2). This is exemplified by 4-nitrophen-yl ethyl(phenyl)phosphinate (9.62), whose (-)-enantiomer was hydrolyzed by rabbit serum arylesterase almost 10 times faster than the (+)-enantiomer [133],... [Pg.584]

M. A. Sogorb, I. Sanchez, M. Lopez-Rivadulla, V. Cespedes, E. Vilanova, EDTA-Re-sistant and Sensitive Phosphodiesterase Activities Associated with Albumin and Lipoproteins in Rabbit Serum , Drug Metab. Dispos. 1999, 27, 53-59. [Pg.603]

Preparation of Rabbit Serum and Antiserum. Four white New Zealand rabbits (2-3 kg) were first bled to obtain normal serum (NS), then injected subcutaneously with a total of 2.5 mg of either f-1, f-3, f-4, or f-5 in complete Freund s adjuvant. [Pg.261]

Figure 2. Double diffusion of cotton dust fractions and cotton bract extract against rabbit antiserum to dust (AD) and normal rabbit serum (NS). Conditions described in Material and Methods.

$Figure 2. Double diffusion of cotton dust fractions and cotton bract extract against rabbit antiserum to dust (AD) and normal rabbit serum (NS). Conditions described in Material and Methods.$

Figure 4. Double diffusion of extracts from cotton plant tissues and extract from flax against rabbit antiserum to cotton dust. Key. a AD,antisera to dust gin, gin trash If, leaf antigen stm, stem antigen cd, cotton dust antigen bet, bract antigen burr, burr antigen, b NS, normal rabbit serum, c fix, flax extract f-4, cotton dust antigen. Conditions described in Material and Methods.

Reactivity Between Rabbit Antisera to Cotton Dust and Bract, Normal Rabbit Serum, and Extracts of Cotton Dust, Cotton Tissues, House Dust, and Certain Bacterial Endotoxins. [Pg.269]

Rabbit antirat IgG (from approx 20 mL rabbit serum). [Pg.24]

In order to investigate the active sites of these proteins, laccases I and III were subjected to ESR (electron spin resonance) spectroscopic analysis. The ESR spectra shown in Figure 5 indicate clear differences in peaks 2 and 6 which support the concept that the copper atoms in laccases I and III have different conformations in each molecule. Furthermore, immunological similarity between laccases I and III was also investigated. Antibody specific for laccase III was prepared from rabbit serum by conventional methods. When applied to Ouchterlony diffusion plates containing laccase I, no precipitation lines developed (Figure 6). This result showed that there were no conserved epitopes on the surfaces laccases I and III. [Pg.211]

Controls with the anti-glycohydrolases IgG, first incubated with the enzymic extract before being applied in thin sections, showed no labeling (Fig. 2B). Other controls performed, i.e., replacement of the primary antibody by normal rabbit serum or preimmune serum, suppression of the first step corresponding to the primary antibody, or labeling of uninfected wood specimen, were also negative. [Pg.446]

Fig. 11a and b. Oscillation patterns recorded from a 6-phosphogluconate dehydrogenase and b rabbit serum transferrin showing rich and highly oriented molecular diffuse scattering features... [Pg.51]

Zhong WZ. Application of solid-phase extraction in the method development for determination of SEP A, an acronym for soft enhancement of percutaneous absorption in human, rat and rabbit serum using GC-FID method. J Pharm Biomed Anal 1998 16(7) 1179. [Pg.35]

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