Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The experimental exposure of the pulpal room of rabbit teeth made it possible to apply an ovalbumin agar gel deposit into the pulpal room and subsequently investigate the immune response. Diffusion of antigen from the agar into environment was proven. After 3 weekly applications 5 rabbits showed hemagglutinating anti-ovalbumin titers between 1:128 and 1:512, while 7 rabbits receiving 10 weekly applications had titers between 1:8000 and 1:128,000. Control rabbits which received the agar deposit alone showed no antibody response. Control rabbits which obtained 3 identical weekly doses of ovalbumin in PBS by subcutaneous injection showed an identical immune response as animals immunized via the pulpal room. Specificity of antibodies was ascertained by passive hemagglutination with control antigens and hemagglutination inhibition. Intradermal injection of ovalbumin in 3 rabbits which obtained pulpal immunization, induced an Arthus reaction. The precipitating property of ovalbumin antibodies and their identity with defined ovalbumin antisera was proven by gel diffusion. The results obtained show, that antigens present in the pulpal room provide a strong immunogenic stimulus.
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PMID:Experimental pulpal immunization. I. Route of application and demonstration of immune response. 13 47

A new fungal immunomodulatory protein (Fip) has been purified from the edible mushroom, Volvariella volvacea, and designated Fip-vvo. Analysis of the purified protein by SDS/PAGE followed by Coomassie Blue staining demonstrated that Fip-vvo is a single polypeptide with an apparent molecular mass of 15 kDa. Periodic acid/Schiff staining showed that this single polypeptide lacks carbohydrates. Using an in vitro bioassay measuring blast-formation stimulatory activity, Fip-vvo was shown to stimulate the maximum proliferation of human peripheral blood lymphocytes at a concentration of 5 microg/ml. Fip-vvo was capable of agglutinating rat red blood cells. Neither haemagglutination nor mitogenic activities were inhibited by mono- or dimeric sugars. In vivo, repeat administration of Fip-vvo greatly reduced the production of BSA-induced Arthus reaction in mice, whereas little effect was observed on the prevention of systemic anaphylaxis reactions. The selectively enhanced transcriptional expression of interleukin (IL)-2, IL-4, interferon-gamma, tumour necrosis factor-alpha, lymphotoxin and IL-2 receptor by Fip-vvo was also demonstrated by reverse transcriptase-PCR. This finding suggests that Fip-vvo exerts its immunomodulatory effects via cytokine regulation. In addition, the complete amino acid sequence of Fip-vvo was obtained by direct protein sequencing. This protein consists of 112 amino acid residues with a blocked N-terminal end and has a calculated molecular mass of 12667 Da not including the N-terminal blocking group. By gel filtration analysis, Fip-vvo exhibited a molecular mass of 26 kDa for the native molecules in PBS. This result indicates that native Fip-vvo is most likely a non-covalently associated homodimeric molecule.
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PMID:Fip-vvo, a new fungal immunomodulatory protein isolated from Volvariella volvacea. 916 52