Rabbit immunization, peptide

Kentolysin Compared to Heliantholysin. Stoichactis helianthus occurs in the Caribbean region whereas another species, Stoichactis kenti is distributed in the Indo-Pacific area. The latter produces a toxin, kentolysin, that is similar to, but not identical with heliantholysin (6). The amino acid compositions of the two polypeptides show a distinct resemblance but appear to differ significantly in number of residues of lysine, methionine, tyrosine and histidine. IgG from a rabbit immunized against heliantholysin neutralizes both heliantholysin and kentolysin, but neutralization of the homologous toxin is more efficient (Table III). It can be seen that in the concentrations used, the IgG failed to neutralize the related lytic peptides of Condylactis gigantea and Epiactis prolifera. 

Sp2/0 Lymphoc 4es of rabbit immuned by prion peptide Sp2/0 X LR interspecific hybridoma - producent of McAb to prions Savenko N. B., Simonova A. S., Djakonov L. P., 2003... 

The future importance of peptide vaccines lies in the fact that one could replace inactivated or attenuated microbial pathogens or toxins, which are high-molecular and therefore difficult to characterize and standardize, by highly specific synthetic peptides. Emini et al.157 have synthesized oligopeptides that prime the rabbit immune system and are effective against poliovirus. The amino acid sequence of the peptide vaccines 63 and 64 originate in the poliovirus VPt protein. 

Figure 4. Demonstration of the specificity of rabbit antibody sc-253. (A) Shows Fos-like immunoreactivity in a normal mouse VNO. (B) Shows little or no immunoreactivity after preabsorption of sc-253 with the immunizing peptide. (C) A goat version of sc-253 (sc-253G) produces Fos-like immunoreactivity that is very similar to that of the rabbit version in (A).

Selsted ME, Siklarek D, Gam T, Lehrer RI. Activity of rabbit leukocyte peptides against Candida albicans. Infect Immun 1985 49 202-206. 

Lehrer RI, Scklarek D, Ganr T, Selsted ME. Correlation of binding of rabbit anulocyie peptides to Candida albicans with candidacidal activity. Infect Immun 1985 49 207-211. 

Since the RIA for bile acids was described in 1973 by Simij oggs et al., several different procedures have been reported in the literature, the main characteristics of which are summarized in Table 1. All methods utilize polyclonal antibodies produced in rabbits immunized with a bile acid coupled to a protein. The carrier protein generally bovine serum albumin, has been covalently linked by a peptide bond on a carboxy group. 

Antimicrobial peptides are also an integral part of mammalian cell-mediated immunity. They are produced by phagocytic cells, particularly neutrophils, and are designate defensins (47). Althou defensin molecules from humans, guinea pigs, rabbits, and rats may vary between 29-34 amino acid residues and differ slightly in sequence, they invariably show conservation in sue cysteine residues which are required for a defmed pattern of disulfide bonds (47). 

Saunders et al. (1997) have raised a polyclonal antiserum using a peptide specific for ER 3. The peptide (CLSKAKRNGGHAPRVLEL) corresponding to amino acids 196-213 of rat ER(3 was conjugated to keyhole limpet hemocyanin and used to immunize rabbits according to standard procedures. Polyclonal IgGs were purified from serum on a Hitrap protein A Sepharose column based on the manufacturer s instruction (Pharmacia). 

To localize ERp on paraffin sections, 65-kDa antirat ER antibodies are used (Upstate Biotechnology, Lake Placid, NY). This antibody is obtained by immunizing rabbits with synthetic peptides representing the N-terminal amino acid residues 46-63 of human ER(3. The deparaffinized sections on slides are placed in the Target Retrieval Solution (pH 6.1)... 

To localize ER[3 in frozen sections, antigen retrieval with heating is not required. 210-180-C050 antibodies (Alexis Corporation, Nottingham, UK) are obtained by immunizing rabbits with synthetic peptides representing the C-terminal amino acid residues 467-485 of human estrogen. 

A new recombinant vaccine has shown promise in vitro and in rabbits. It combines segments of 21 different immunogenic peptides from P. falciparum into a single recombinant protein, ehciting a multilayered immune response, including B cell and T cell responses (1). 

Results of DEAE-anion exchange chromatography are shown in Figure 1. Partially purified BT israelensis crystal proteins (25 to 28 kilodalton peptides) were used in the immunization of rabbits. Western Blotting (Figure 2) showed that this antiserum reacted strongly with the 25- to 28- kDa peptides. Cross reactivity with the other BT israelensis crystal proteins and the BT kurstaki toxin was minimal. 

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