Protein rabbits

Ih Chemical changes in ground substance and lung protein Rabbit 26... 

Increased serum trypsin protein Rabbit esterase... 

Micrococcus lysodeikticus cells (lysozyme lysate) D-Mannan-protein complex Saccharomyces cerevisiae) Modulator protein (rabbit skeletal muscle)... 

Assuming that approx 5% of the bacterial lysate or pellet is composed of the recombinant protein, and 200 mg are loaded onto the gel, it can be estimated that approx 10 mg of recombinant protein is present in the excised gel slice. It IS suggested that adjustments be made in the amount of protein loaded based on your estimate of the percent of expressed protein in your lysate, such that the band excised contains approx 10 mg protein. The resulting emulsion can be utilized for the immunization of three rabbits, each rabbit receiving approx 3 mg of protein For the first two immunizations, 3-4 mg of protein/rabbit are appropriate. The boosting immunizations require only half of this amount... 

Kabat (251) was able to show by immunochemical methods that the main component of the serum of case 11 (Table VII) was, in fact, a Bence-Jones protein. Rabbit antiserum to this patient s urinary Bence-Jones protein gave a strong precipitin reaction with a 1 625 dilution of the patient s serum. This reaction appeared to be due entirely to Bence-Jones protein since after absorption of the rabbit antiserum with case 11 myeloma serum no additional precipitin reaction could be obtained with the patient s urine or purified Bence-Jones protein nor did the (absorbed) antiserum react with normal serum protein constituents. Qualitative dilution tests indicated a concentration of Bence-Jones protein in the serum of the same order of magnitude as was obtained for the main abnormal component by other methods. In case 1 (Table VII) Kabat was also able to demonstrate by immunochemical methods that while the main component was not a Bence-Jones protein, 0.15 to 0.2 gram per cent of a Bence-Jones protein nevertheless was present and could be identified and estimated by emplojdng the quantitative precipitin method. This concentration, approximately 1.5% of the total protein content of this serum, obviously could not be detected by salting-out, electrophoretic, or ultracentrifugal methods. 

This experiment describes the adaptation of the bicinchoninic acid (BCA) protein assay to a flow injection analysis. The assay is based on the reduction of Cu + to Cu+ by the protein, followed by the reaction of Cu+ with bicinchoninic acid to form a purple complex that absorbs at 562 nm. Directions are provided for the analysis of bovine serum albumin and rabbit immunoglobulin G, and suggestions are provided for additional analyses. 

Fibers (see Fibers, survey) used in textile production can have a wide variety of origins plants, ie, ceUulosic fibers (see Fibers, cellulose esters) animals, ie, protein fibers (see Wool) and, in the twentieth century, synthetic polymers. Depending on the part of the plant, the ceUulosic fibers can be classified as seed fibers, eg, cotton (qv), kapok bast fibers, eg, linen from flax, hemp, jute and leaf fibers, eg, agave. Protein fibers include wool and hair fibers from a large variety of mammals, eg, sheep, goats, camels, rabbits, etc, and the cocoon material of insect larvae (sUk). Real sUk is derived from the cocoon of the silkworm, Bombjx mori and for a long time was only produced in China, from which it was traded widely as a highly valuable material. 

Species origin tests, used to determine whether the specimen is human or from another source, are immunological in nature. Host animals, usually rabbits, are injected with protein from another species. The animal creates antibodies to the unknown material. Semm from the host animal, containing species (human, bovine, equine, canine, etc) specific antibodies, is tested against a dilute solution of blood (antigens) collected as evidence. A positive reaction is determined by a visible band where the antibodies and antigens come into contact. 

Metallothionein (from rabbit liver) [9038-94-2], Purified by precipitation to give Zn- and Cd-containing protein fractions and running on a Sephadex G-75 column, then isoelectric focusing to give two protein peaks [Nordberg et al. Biochem J 126 491 1972]. 

Myofibrillar Structural Proteins of Rabbit Skeletal Muscle ... 

Jervis used porous silica coated with chemisorbed polyacrylhydrazide for immobilization of adenosine monophosphate (AMP) [117]. After periodate oxidation of its ribose residue the ligand was coupled to the carrier and used for isolation of lactate dehydrogenase from rabbit muscle. The specific capacity was 2 mg of protein/g adsorbent with a ligand content of 10 pmol/g, whereas recovery of enzymatic activity after elution was 85%. Hipwell et al. [118] found that for effective binding of lactate dehydrogenases on AMP-o-aminoalkyl-Sepharose the spacer arm length required at least 4 methylene links. Apparently, a macromolecule of polyacrylhydrazide acts itself like an extended spacer arm and thus allow AMP to bind the enzyme. 

Xu, Q. et al. (1992). Induction of arteriosclerosis in normocholesterolemic rabbits by immunization with heat shock protein 65. Arterioscler. Thromb. 12, 789-799. 

The mature red blood cell cannot synthesize protein. Reticulocytes are active in protein synthesis. Once reticulocytes enter the circulation, they lose their intracellular organelles (ribosomes, mitochondria, etc) within about 24 hours, becoming young red blood cells and concomitandy losing their ability to synthesize protein. Extracts of rabbit reticulocytes (obtained by injecting rabbits with a chemical—phenylhydrazine—that causes a severe hemolytic anemia, so that the red cells are almost completely replaced by reticulocytes) are widely used as an in vitro system for synthesizing proteins. Endogenous mRNAs present in these reticulocytes are destroyed by use of a nuclease, whose activity can be inhibited by addition of Ca +. The system is then pro-... 

An increased level of exploratory activity immediately after exposure, attributed to reduced anxiety on the part of the rats, was also observed in this study. Decreased avoidance was observed in rats exposed to 125 ppm trichloroethylene 4 hours per day, 5 days per week for 30 days (Goldberg et al. 1964a). Changes in visually evoked potentials (Blain et al. 1992) and electroretinal responses to flash stimulation (Blain et al. 1994) were seen in rabbits exposed to 350 ppm trichloroethylene for 12 weeks (4 days/week, 4 hours/day). The study authors suggested that binding of trichloroethanol to blood proteins may enable it to reach the visual cortex. 

Polyclonal Antibodies against FORL r purified polygalacturonase were raised in white rabbits. For the first immunization 200 jxg of purified protein in 300 jxl of distilled water was mixed with 200 1 of PBS and 500 n of complete Freund s adjuvcmt and injected intramusculary into the leg. Two subsequent intramuscular injections, each containing 300 fig of protein in 1 ml of incomplete Freund s adjuvant were given at 1 month intervals. Finally, the rabbit was bled 1 week later. The antisera, separated from blood by incubation at 37 "C, were stored in 1 ml fractions at -20 C. 

---