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Rabbit serum albumin

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]

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]

The ELISA procedure recently has been used for the analysis of parathion (31). Since this procedure has considerable potential a more detailed description of the analysis of parathion is in order. The conjugation procedure using amino parathion (AP) was described earlier (Fig. 3, Rn 9), and this conjugate was then administered to rabbits for development of a population of specific antibodies (Abi) against BSA or AP. Abi demonstrated immunological activity only for the hapten when AP was conjugated to rabbit serum albumin (RSA). This antigen (RSA-AP) was rendered insoluble via attachment to the polystyrene surface of microtiter plates under basic conditions (Fig. 6.1). [Pg.339]

CO) polystyrene surface (RSA) rabbit serum albumin (AP) conjugated aminoparathion (Ab,) first antibody (rabbit anti-parathion) (Abz) second antibody (goat anti-rabbit) (E) enzyme (horse-radish peroxidase) (S) substrate and (P) free hapten (parathion). [Pg.340]

The binding of sulfonamides to serum albumin is thought to strongly affect the pharmacokinetics of drug action, and therefore CD spectroscopy has been used to deduce the nature of the association mechanism [71]. It was found in this study that most of the drug compounds would exhibit induced CD upon binding to either human, bovine, or rabbit serum albumin, and that the particular lineshape of the chiroptical spectrum was determined by the structural details of the bound solute. [Pg.327]

The following binding data have been obtained between cefotaxime and rabbit serum albumin ... [Pg.192]

They experimented with four other proteins as carriers rabbit serum albumin, bovine serum albumin, bovine fibrinogen fraction I, and bovine )8-globulin fraction III. The structurally related derivatives of DDT and malathion, DDA, and 0,0-dimethyl S-carboxy-carboxyethyl phosphoro-dithioate (malathion half ester), respectively, were used as the specific haptens attached to these carrier proteins. These compounds contain free carboxyl groups, which when they reacted with thionylchloride, provide a means of coupling of the hapten to the amino groups of the protein carrier. [Pg.168]

After 2 hours the mixture was dialyzed against 10 mM sodium phosphate (pH 7 4) containing 0.022 sodium azide. The substitution ratio of the clomazone analog to BSA was calculated to be 19 2 using the equations of Fenton and Singer (12) with the assumption of no loss of protein. A rabbit serum albumin (RSA) conjugate was prepared by the same procedure, except the concentration of RSA used in the coupling step was 20 mg/mL, and yielded a substitution ratio of 2.4. [Pg.171]

F9. Fleischer, 8., and Haurowitz, F., The metabolism of homologous TCA -rabbit serum albumin. Arzneimittel-Forach. 10, 362-363 (1960). [Pg.287]

Histamine-rabbit serum albumin conjugate Immunoglobulin E... [Pg.596]

Ben-Ephraim S, Arnon R, Sela M (1966) The immune response of inbred strains of guinea pigs to polylysyl rabbit serum albumin. Immunochemistry 3 491-494 Berglund G (1965) Preparation of antiserum to an antigen of low molecular weight. Nature... [Pg.28]

The rabbit serum albumin was prepared by Dr. George A. Feigen, by a single salt precipitation. [Pg.130]

Rabbits are immunized with DNP-bovine serum albumin and goats with DNP-keyhole limpet hemocyanine. All animals are immunized by two injections, 3 weeks apart. Each injection consists of 1 mg of the antigen in 1 ml of a buffer composed of 0.15 M NaCl and 0.01 M sodium phosphate (pH 7.4) emulsified with 1 ml of complete Freund s adjuvant (Difco). Injections are given at several intradermal sites. Animals are bled weekly after the second injection and, when antibody titers decrease to below 0.5 gm/ml, are boosted by reinjection in the same manner. Rabbit antisera are pooled whereas the antiserum of each bleeding from each goat is separately maintained. Anti-DNP antibodies are isolated on a DNP rabbit serum albumin-Sepharose immunoadsorbent. The adsorbed antibodies are eluted by incubation (1 hr) with 0.1 M acetic acid at 37° and dialyzed against a buffer composed of 0.01 M sodium phosphate and 0.15 M NaCl (pH 7.4). The myeloma protein 315 is isolated from the serum of tumor-bearing mice by a described procedure. ... [Pg.491]

Fig. 2.4. Inhibition by alanine peptides of the precipitates obtained by reacting (A) IgG obtained from anti-poly-L-alanyl-human serum albumin with poly-L-alanyl-rabbit serum albumin (B) IgG obtained from anti-poly-o-alanyl-HSA with poly-D-alanyl-RSA. L, L-alanine D, D-alanine L2 is the polymer containing two L-alanine groups, etc. Reprinted by permission from Schechter et at. (22). Fig. 2.4. Inhibition by alanine peptides of the precipitates obtained by reacting (A) IgG obtained from anti-poly-L-alanyl-human serum albumin with poly-L-alanyl-rabbit serum albumin (B) IgG obtained from anti-poly-o-alanyl-HSA with poly-D-alanyl-RSA. L, L-alanine D, D-alanine L2 is the polymer containing two L-alanine groups, etc. Reprinted by permission from Schechter et at. (22).

See other pages where Rabbit serum albumin is mentioned: [Pg.242]    [Pg.245]    [Pg.286]    [Pg.232]    [Pg.327]    [Pg.193]    [Pg.175]    [Pg.162]    [Pg.169]    [Pg.68]    [Pg.12]    [Pg.21]    [Pg.492]    [Pg.8]    [Pg.146]    [Pg.45]    [Pg.32]    [Pg.174]   
See also in sourсe #XX -- [ Pg.748 ]

See also in sourсe #XX -- [ Pg.422 ]

See also in sourсe #XX -- [ Pg.422 ]




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