Ovalbumin activity

A, B, and C, surrounded by a helices. The polypeptide chain is colored in sections from the N-terminus to facilitate following the chain tracing in the order green, blue, yellow, red and pink. The red region corresponds to the active site loop in the serpins which in ovalbumin is protruding like a handle out of the main body of the structure. (Adapted from R.W. Carrell et al.. Structure 2 257-270, 1994.)... 

The flexible loop region in the active form of antithrombin (Figure 6.23a) is in the same general position as in ovalbumin but the first few residues form a short sixth p strand in p sheet A inserted between strands pS and pis. Furthermore there is no a helix in the loop which is extended outside the main body of the molecule, ready to be inserted into the active site of thrombin. 

GME glycine methyl ester GDM glutamic dimethyl ester EDA ethylendiamine GAM glucosamine HDA hexadecylamine BSA bovine serum albumin OVA ovalbumin CA carbonic anhydrase MYO myoglobin H alkaline hydrolysis for converting ester groups from GME or GDM into free carboxylic acid groups that were subsequently activated with EDC for further modifications. 

Figure 3. (A) Determination of molecular mass of pectic enzymes by gel filtration in Sepharose 6B. Molecular mass markers - tyroglobulin, 2- apoferritin, 3- p-amylase, 4-alcohol dehydrogenase, 5- bovine serum albumin, 6- carbonic anhydrase. (B) SDS-PAGE of pectolytic activities. Molecular mass markers 1- myosin, 2- p-galactosidase, 3- phosphorylase b, 4- bovine serum albumin, 5- ovalbumin, 6- carbonic anhydrase.

Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])...

FIGURE 7.7 (See color insert) Adoptively transferred D011.10 transgenicT cells can be identified by expression of CD4+ and KJ-126 in spleen cell suspension from Balb/c mice after ovalbumin (OVA) immunization. Balb/c mice were injected iv with D011.10 spleen cells containing 3-5 x 1 06CD4+KJ-126+ cells and immunized by intraperitoneal injection of 2 mg OVA emulsified in complete Freund s adjuvant 2 days later. OVA immunization increases the frequency of KJ+T cells and alters the expression of various surface molecules consistent with T cell (Tc) activation. 

Nickel significantly enhanced the synthesis and/or secretion of IL-2 by cultured murine splenocytes and also the expression of the receptor for IL-2 [386]. It was also shown [387] that nickel increased IL-2 production in an antigen-specific (ovalbumin) T cell activation system in vitro. 

The enzymes used by these workers were cholinesterase, prepared from horse serum, and horse-liver esterase. Parallel experiments were carried out with twice crystallized ovalbumin, and with an aged, dialysed specimen of horse serum with negligible esterase activity. 

As a variant, activate the peptide separately first and couple then to the carrier Dissolve the peptide to 1 mg/ml in ddH20, add 10 mg EDAC hydrochloride per milligram of peptide, and adjust pH to 5.0. Incubate at RT for 5 min and correct the pH with diluted NaOH during this period. Then add the same volume of carrier protein solution. The amount of carrier protein should be in a ratio of 40 moles of COOH groups per mol peptide (ovalbumin 42.7 kD, 31 Asp, 48 Glu/Mole BSA 67.7 kD, 54 Asp, 97 Glu/Mole). Shake at RT for 4 h and stop the reaction by addition of 1/10 volume of 1 M sodium acetate buffer, pH 4.2. Free the sample from surplus reagents by gel filtration or dialysis and concentrate to about 1 ml by ultrafiltration. 

Dissolve 5 mg of ovalbumin, BSA, or another suited carrier protein in 100 pi ddH20. The pH has to be 6, because aggregation occurs above pH 7. Add Soln. B to a final concentration of 2.5% giutaraidehyde and stir at RT for 30 min. Filtrate the reaction mixture on a PD-10 or Sephadex G-25 column, equilibrated with ddH20, and collect the activated protein in the void volume. ... 

Dissolve the required amount of peptide (1 mole peptide per about 50 moles of lysine residues of the carrier, e.g., 60 pmol of peptide per 5 mg ovalbumin) in PBS and mix with the activated carrier. Stir at RT for 1 h and block with 10 mg/ml of solid NaBH4 at RT for 20 min. Alternatively, reduce (block) the formed azome-thines (Schiff bases) to secondary amines by addition of ascorbic acid (final concentration 5 mM). 

Antigen expression inhibition. Fresh plant juice, in the ration of female mice, was active vs IgE antibody expression in ovalbumin-sensitized mice° h Antihalitosis effect. Dried root ingested by adults was active. The biological activity has been patented ". 

Immunostimulant activity. Fresh plant juice, in the ration of female mice, was active in ovalbumin-sensitized mice . Water extract of the dried root, taken orally by human adults, was active. A pharmaceutical solution containing fruit bodies of Tremella fuciformis, Daucus carom root, Astragalus mongholicus root and Zizyphus jujuba fruits, honey, vitamin A palmitate, zinc sulfate, and vitamin C is claimed useful as an immunostimulant for controlling AIDS, cancer, and infections L Inotropic effect (negative). Ethanol (80%) extract of the aerial parts, at a concentration of 0.3 mg/mL, was active on the guinea pig atrium . 

Osteoclast. A large multinuclear cell associated with the absorption and removal of bone, osteoclasts become highly active in the presence of parathyroid hormone, causing increased bone resorption and release of bone salts (phosphoms, and especially calcium) into the extracellular fluid. Ovalbumin. An albumin obtainable from the whites of eggs. 

The presence of oxygen was shown to enhance inactivation of the enzyme, while the presence of ovalbumin in the phenolase solution protected the activity. This was accepted as evidence that indirect action of the radiation was responsible for the inactivation of phenolase since the presence of dissolved oxygen or protein would have no effect on direct collisions of the 7-rays and the enzyme molecules. 

Fig. 1.4 The bronchoconstrictor effects of adenosine, NECA, CPA, CGS 21680 and 2-C1-IB-MECA in actively sensitised, Brown Norway rats 3 h post intratracheal instillation of vehicle (saline, 0.2 ml) or ovalbumin (OA, 0.3 mg kg-1). The agonists were given i.v. and to avoid tachyphylaxis, only one response was generated per animal. Results are expressed as means s.e. means (n = 4—5). P < 0.01, P < 0.001 that the value is significantly different from the equivalent value in the vehicle-challenged group (from Hannon et al. 2002b, with permission)...

Fig. 1.6 Effect of adenosine, CPA and 2-C1-IB-MECA at the concentrations indicated on lung parenchymal strips prepared from actively sensitised Brown Norway rats 3 h post intratracheal instillation of ovalbumin (0.3 mg kg 1 filled columns) or saline (open columns). Responses are expressed relative to the response to bethanechol (100 pM) which was taken as 100%. Mean values ( SEM) from the number of individual experiments shown in parentheses are presented. P < 0.05, P < 0.001 that the value differs significantly from the equivalent value in the saline challenged group (from Wolber and Fozard 2005, with permission)...

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