Among the highly heterogeneous components of the mouse urinary protein complex (MUP) a hydrolase was detected which was capable of spliting the proteinase ester substrate TAME as well as a synthetic chromogenic tripeptide specific for tissue and urinary kallikreins. The binding of mouse-specific IgE antibodies from the serum of a highly mouse-allergic patient occurred preferentially to this kallikrein-like enzyme. This finding underscores the possible association of significant biological activities with predominant IgE-binding allergens, especially in view of the strongly sensitizing potential and the known messenger functions of the MUP proteins.

Alpha-Globulins↗

PubMedDate not supplied

Detection of class-specific antibodies against Aspergillus fumigatus antigens in various pulmonary diseases.

Using an enzyme-linked immunosorbent assay (ELISA) and a radioimmunoassay (RAST), the specific IgA, IgG, IgM and IgE antibody levels against Aspergillus fumigatus antigens were determined in sera from patients with either chronic bronchitis or non-allergic bronchial asthma, allergic asthma, allergic bronchopulmonary aspergillosis or aspergilloma. These levels were compared with those in serum samples from healthy controls. The results showed statistical differences in specific antibody levels between the five groups of patients. It was not possible, however, to reliably classify a subject in one of the studied pathological groups on the sole basis of the assays used.

Antibodies, Fungal↗

PubMedDate not supplied

Chemical nature of antioxidant complement activators in allergenic extracts.

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Allergens↗

PubMedDate not supplied

Haptenic side chains as posttranslational IgE-binding determinants among pollen protein allergens.

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Allergens↗

PubMedDate not supplied

Complement, IgE- and IgG4-antibodies in the diagnosis of atopic diseases.

Haemolytic complement (C) in human sera is readily consumed by most of the common inhalant allergens. The reactivity of C among individual sera differs considerably and is a characteristic parameter for the condition of atopy. The phenomenon is not mediated by specific IgE or IgG4 antibodies. Whereas in groups of patilues (by RAST) are negative in about 50 percent of the cases, this is not so with regard to C-reactivity. In somes cases, especially in allergy to guinea pigs, correlation with the clinical history is better with IgG4 than with IgE antibodies. In other allergies, there is a close correlation between Ige and IgG4 antibodoes.

Animals↗

PubMedDate not supplied

Complement consumption and IgE binding by house dust allergen in the serum of atopic patients.

The reactivity of complement (C) with housedust allergen has been investigated in separate groups of sera from atopic patients with seasonal hay fever, bronchial asthma, atopic dermatitis, animal dander allergy or asthmatic bronchitis as compared to controls. Complement consumption was more pronounced on average in the allergy groups, with the exception of atopic dermatitis. Total IgE levels were elevated in all groups, especially in atopic dermatitis. There was no correlation between C-sensitivity and IgE data (RAST and RIST). The mean levels of C1-inhibitor, 1-antitrypsin and 2-marcroglobulin in the atopic group were found normal. A significant correlation was found between the extent of C-consumption by house dust allergen and the level of C4 in sera. It is concluded that both C and IgE differ from normal in atopic patients, but that neither one is suited for the routine diagnosis of atopy in individual serum samples.

Adult↗

PubMedDate not supplied

Comparative studies of allergenic extracts prepared from freshly collected, dried, or dried and defatted pollen.

Fresh pollen samples of Parietaria judaica, Betula pubescens, Dactylis glomerata and Olea europaea were collected and aliquot portions of these pollens were stored after drying in hot air, while other portions were dried and then defatted with diethylether. The different pollen materials were extracted with aqueous media to obtain the non-dialyzable allergenic protein constituents. Review of the production data, together with comparative analyses of the UV-absorption spectra and of IgE binding potencies did not reveal appreciable differences in allergen composition among extracts of fresh, dried, or dried and defatted pollen materials. However, microscopic examination showed the fresh pollen to be no longer viable.

Binding Sites, Antibody↗

PubMedDate not supplied

Enzymatic methods for the evaluation of the allergenic potency of house dust extracts.

House dust extracts are known to contain powerful proteolytic enzymes. The significance of these proteases is supported by the recently reported association of major dust mite allergens with serine and/or cysteine proteases. The proteolytic activity of house dust extracts, therefore, represents an allergologically relevant parameter for mite-derived allergens. However, several other major allergens in extracts of animal and insect excreta (e.g., from cockroaches) have been shown to possess protein hydrolase properties. Furthermore, acid phosphatase activities are known to correlate well with allergenic potency in several pollen extracts. The present study reports on the quantitative estimation of these two enzymes in relation to human antimite IgE-binding potency in 20 different dust samples from Spanish houses.

Acid Phosphatase↗

PubMedDate not supplied

Investigation of acid phosphatase as a possible IgE-binding marker for pollen allergens and their polymerized derivatives.

The enzyme acid phosphatase represents an important component among the allergenic proteins in most pollen extracts. However, determination of the level of this enzyme in extracts of various pollen species, as well as protein separation by molecular sieving shows that acid phosphatase cannot be used as a marker for IgE-binding protein allergens. A conspicuous discrepancy was observed between the heat- and acid-sensitivities of the phosphatase enzyme relative to the overall IgE-binding properties of the pollen extracts. Remarkably, the enzyme remained unaffected by cross-linking the pollen proteins with glutardialdehyde, whereas this process of polymerization caused the IgE-binding potency to diminish considerably. It is concluded that the enzyme acid phosphatase is not a suitable marker for the potency assessment of pollen allergens, but may be useful for monitoring the production process of polymerized allergoids.

Acid Phosphatase↗

PubMedDate not supplied

The role of IgG in type-I allergy: an unsolved problem.

The role of antiallergen IgG antibodies in allergy remains unclear. In this review we present evidence for and against the hypothesis that IgG (IgG4) could act as a sensitizing antibody. After considering the available data, we conclude that the possible sensitizing ability of IgG4 may depend on the nature and origin of the antibodies and cells used in the various experiments and/or is related to the differential induction of two subtypes of IgG4 (anaphylactic vs. blocking). It still remains to be settled whether the observed increase in specific IgG during immunotherapy is causally related to the relief of symptoms, or whether it merely represents an epiphenomenon due to high antigen exposure. Furthermore, the presence of IgG anti-IgE antibodies in the serum of allergic patients and their possible pathophysiological relevance is discussed in the light of recent evidence suggesting that the raised levels of these antibodies may likewise represent an epiphenomenon of the immune response. There exists a tight relationship between antiallergen IgE and IgG antibodies. This correlation has led to the suggestion that IgG determinations might be useful for diagnostic purposes. There also exists a good correlation between these antiallergen isotypes in inhibition assays. It has therefore been proposed to employ inhibition of IgG binding for the standardization of allergenic extracts. More recent studies explore the relevance of the binding affinities or avidities of allergen-specific IgG antibodies. Antibody affinity may have important repercussions with respect to the biological effects. It has been pointed out that the affinity of specific IgG subclasses in allergic patients depends, among other things, on the nature of the sensitizing allergen. Further studies on IgG binding to the so-called "major" and "minor" allergens may help clarify the role of IgG in allergic disorders.

Animals↗