Chicken gels from

Fig. 6. Purified recombinant HMGA proteins bind to four regions of DNA on random sequence nucleosome core particles. Panel A The results of EMSA gel assays in which increasing concentrations of either purified nonhistone HMGN2 (a.k.a., HMG-17, which binds to two sites on nucleosome core particles) or recombinant human HMGAla protein were bound nucleosome core particles isolated from chicken erythrocytes [57]. Panel B Two different views of the nucleosome taken from the X-ray structure of Luger et al. [119] showing the sites of binding of HMGA proteins (dashed circles) determined by DNA foot-printing analyses and other techniques (see text for details).

Fig. 10. A. Acetic acid-urea-triton-X-100 polyacrylamide gel electrophoresis [15] of the histones used to reconstitute 208-12 nucleosome arrays consisting of recombinant H2A.Z (lane 2) or recombinant H2A.1 (lane 3). Lanes 1 and 4 respectively are chicken erythrocyte and calf thymus histones used as markers [42]. B. Ionic strength (NaCl concentration) dependence of the average sedimentation coelRcient (s2o,w) of reconstituted 208-12 nucleosome arrays containing either H2A.1 (O) or H2A.Z ( ) [42]. The dotted line represents the behavior of a 208-12 complex reconstituted with chicken erythrocyte histones [406]. [Reproduced from Abbott D.W. et al. (2001) I. Biol. Chem. 276, 41945-41949, with permission from The American Society for Biochemistry and Molecular Biology.]...

BDE 17, 28, 47, 66, 85, 99, 100, 153, 154 183 Adipose tissues from marine mammals, chicken and trout Adipose Tissues, chicken and trout MSPD with silica gel/anhydrous sodium sulfate powder, purification thorug GPC extraction with 400 mL of 1 1 (v/v) acetone/hexane mixture Gas Chromatography (VF-5MS Eactor Eour, Varian) IT-MS 0.07-1.3 pg (instrumental limit of detection) [42]... 

Figure 6.20 Photographs of variously prepared egg white gels. (A) A hard-boiled fiesh egg pickled for 23 days in 0.9 M NaOH + 0.5 M NaCl solution. The laser light (X = 660 nm) shows that the initial white egg gel becomes transparent (B) A fresh chicken egg incubated in a similar NaOH-NaCl solution for 15 days. (C) Another fresh chicken egg incubated for 15 days in a 0.9 M KOH + 0.5 M KC1 solution. (D) A slice of a fiesh chicken egg gel prepared in the same way as before which remains transparent after boiling for 10 min in H20. Reproduced from Eiser et al. (2009) with permission.

Vanillin in MeOH and sulphuric acid was used for the derivatization of MON. Chicken tissue (muscle, liver, skin with adhering fat tissues) samples were homogenized with MeOH-water, NaCl was added to the supernatants, and MON was isolated and concentrated by liquid-liquid partition carbon tetrachloride and by SPE on the silica gel. Standard recoveries ranged from 82% to 96%. The method is specific for MON in the presence of closely related PETs— NAR and SAL. Lasalocid and other antibiotics, such as tylosin, nicarbazin, bacitracin, lin-comycin, and bambermycin, do not react in the system and therefore do not interfere (102). A similar method was also used for the determination of MON in bovine tissues and milk. The homogenization of milk was performed by using MeOH. Recoveries achieved were 79-88% with RSD values of 4.6-9.1% (103). 

Suitable matrices are available from a number of suppliers and include T-gel adsorbent (Pierce). Amersham Biotech offers HiTrap IgM and HiTrap IgY aimed at the purification of IgM and the chicken immunoglobulin, IgY. These are based on 2-mercapto-pyridine as the thiophilic adsorbent. 

Chicken egg white lysozyme (LZM) does not possess exposed methionyl residues, and it has six tryptophan residues, three of which, located at positions 62,108, and 111 are readily oxidizable with ozone and are built-in the LZM active center (D14). Tryptophanyl residues are also the first reacting moieties upon treatment of LZM with the MPO-Cr-H2C>2 system (at pH 4.5). The reaction occurs in several stages. In the first stage, which occurs when 1.4-1.8 mol of H2O2 for 1 mol of LZM is used, LZM loses its enzyme activity, but no derivative distinguishable from the native protein on the polyacrylamide gel electrophoresis is formed. The inactivation may be prevented by addition to the reaction medium A-acetylcysteine or... 

Fig. 9. Effect of CsA on the rate of procollagen 1 triple helix formation in suspended chicken embryo tendon cells. The time course of procollagen 1 triple helix formation was monitored in a pulse-chase experiment by separation of protease-resistant al(l) and a2(I) chains by SDS-polyacrylamide gel electrophoresis. The fluorograms (upper panel) show the appearance of protease-resistant and hence triple-helical collagen I in the absence (—) or in the presence (-I-) of 5 fiM CsA. The kinetics are shown in the lower panel (O) no CsA ( ) 5 ixM CsA. Best fits are drawn according to the model of Bruckner and Eikenberry (1984). From Steinmann et al. (1991).

Superabsorbent polymers are used as a liquid-absorber in food packaging systems. In these systems, the superabsorbent polymers absorb juice or water from fresh foods such as raw chicken, shellfish, and other meats or from frozen foods as they thaw. Chilled superabsorbent polymer gels may also be used as a dry-cooling medium. The water-swollen gel, contained in a durable plastic bag, is frozen and used to keep perishable foods cold. In addition to its liquid-water-absorption characteristic, superabsorbent polymers absorb water from the vapor state and therefore may be used to control humidity. 

Early in the study of the enzymology of the biosynthesis of HMG-CoA, there was some confusion as to whether these processes were physically separated within the cell. Studies by Lane and his collaborators [13] and by others [14] clearly indicated a duality of locus. The cytosolic enzyme, purified from avian liver [13], was found to have a molecular weight of 1.7 x 10 with 4 apparently identical subunits (41000 by SDS gel electrophoresis). The cytosolic enzyme constituted 70% of total thiolase found in chicken liver. 

FIGURE 1 Sodium dodecyl sulfate-polyarcylamide gel electrophoresis of equine platelet pp-TM (lane 1), rabbit skeletal muscle cta-TM (lane 2), rabbit skeletal muscle pp-TM (lane 3), and chicken gizzard TM (lane 4). Note that the chicken gizzard TM is composed of two subunits a and P in a molar ratio of 1 1. This figure is adapted from Fig. lb of Lau et al., (1985), in which the a-TM chain was inappropriately designated y-TM. 

CP from all species analyzed so far occurs as multiple basic isoforms with isoelectric points around 9 (Takahashi et al, 1988a). Using two-dimensional (2D) gel electrophoresis it has been established that CP is expressed in up to three major isoelectric variants (a, P, 7 see Fig. 2) of similar molecular mass, ranging from pi s of 9.9 to 9.4 (Gimona et al, 1992). The isoforms appear progressively with the differentiation in chicken gizzard, porcine stomach (Gimona et al,... 

FIGURE 2 Silver-stained mini 2D gel of chicken gizzard smooth muscle showing the three isoelectric variants (a, (B, y from right to left) of CP expressed in this tissue type. 

Figure 5,8, CsCI profiles of compositional DNA fractions from human placenta, B mouse liver and C chicken erythrocyte, as obtained from preparative centrifugation in CS2SO4/BAMD density gradient. The rf (ligand/tiueleotide molar ratio) values used were 0.12 for mouse and 0.14 for human and chicken. Modal buoyant densities and relative amounts of the fractions arc indicated. P indicates the pellet. Notice the satellite peak (centered at abt>ut 1.700 g/ml) in the last fractions of human, and the satellite peak (1.691-1.692 g/cm ) in mouse DNA fractions i-4. A , B and C display autoradiograms of terminally labelled (Cooper et al.. 1983 1.2% agarose gels were used) Hpa 11 fragments from DNA fractions. (From Aissani...

HMG-CoA synthase (EC 4.1.3.5), catalyzing the formation of HMG-CoA and CoASH from acetyl-CoA and acetoacetyl-CoA, and not yet characterized from plants, was partially purified from C. roseus. It is an unstable enzyme that is rapidly inactivated in the presence of a relatively high concentration of salt (>200 mM). Thus far it has not been separated from AACT (81). HMG-CoA synthase activity elutes from gel filtration columns (e.g., Superose 6) with a retention time similar to that of polypeptides with an M, of about 100 kDa. HMG-CoA synthases isolated from other eukaryotic sources are mostly dimeric proteins of which the subunits have M, of 50-55 kDa for example, HMG-CoA synthase from chicken liver consists of two subunits of 53 kDa (82). When L-659,699, a /3-lactone inhibitor of mammalian cytosolic HMG-CoA synthase isolated from, among other sources, Fusarium sp. (83), is added to suspension cultured cells of... 

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