WO1982001132A1 - Lower allergenicity and lower thrombogenicity foodstuff and process for preparing the same - Google Patents

Lower allergenicity and lower thrombogenicity foodstuff and process for preparing the same Download PDF

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Publication number
WO1982001132A1
WO1982001132A1 PCT/US1981/001353 US8101353W WO8201132A1 WO 1982001132 A1 WO1982001132 A1 WO 1982001132A1 US 8101353 W US8101353 W US 8101353W WO 8201132 A1 WO8201132 A1 WO 8201132A1
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glycoprotein
coffee
glycoproteins
cocoa
tgp
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PCT/US1981/001353
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English (en)
French (fr)
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Res Foundation Inc Cornell
C Becker
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Res Foundation Inc Cornell
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Priority to DE19813152395 priority Critical patent/DE3152395A1/de
Publication of WO1982001132A1 publication Critical patent/WO1982001132A1/en

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    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
    • A23G1/00—Cocoa; Cocoa products, e.g. chocolate; Substitutes therefor
    • A23G1/02—Preliminary treatment, e.g. fermentation of cocoa
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23F—COFFEE; TEA; THEIR SUBSTITUTES; MANUFACTURE, PREPARATION, OR INFUSION THEREOF
    • A23F5/00—Coffee; Coffee substitutes; Preparations thereof
    • A23F5/16—Removing unwanted substances
    • A23F5/18—Removing unwanted substances from coffee extract
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
    • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K39/00—Medicinal preparations containing antigens or antibodies
    • A61K39/35—Allergens
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

Definitions

  • U.S. Patent 3,997,685 Strobel deals with obtain- ing various aroma and flavor products from substrates bearing the same, typically ground, roast coffee.
  • ground, roast coffee is contacted with cold, wet steam whereby water-soluble constituents are essentially leached from the ground, roast coffee and, following separation and collection of flavor and aroma concentrates, are eventually condensed to obtain what Strobel et al characterize as a liquid flavor concentrate.
  • Such a liquid flavor concentrate, and later products obtained per Strobel et al which com- prise an aqueous system can be subjected to the pro ⁇ cess of the present invention.
  • U.S. Patent 4,006,263 Klug et al discloses a method for removing polyhydroxy phenols and polyhy- droxy phenol-polysaccharide materials from a coffee extract which react with elemental iron to form an unpleasing precipitate.
  • the coffee extract which is processed per Klug et al to permit precipitation of iron reactive compounds can be subjected to the pro ⁇ cessing of the present invention to remove glycopro- tein therefrom before, during or after the processing of Klug et al, i.e., while present as an aqueous system.
  • U.S. Patent 4,081,561 Meyer et al relates to a process of producing partially decaffeinated soluble coffee. At numerous stages in the Meyer et al process an aqueous extract, which may be dilute or relatively concentrated, exists; such aqueous extracts can be processed per the present- invention to remove glyco ⁇ protein therefrom.
  • U.S. Patent 4,081,561 Meyer et al relates to a process of producing partially decaffeinated soluble coffee. At numerous stages in the Meyer et al process an aqueous extract, which may be dilute or relatively concentrated, exists; such aqueous extracts can be processed per the present- invention to remove glyco ⁇ protein therefrom.
  • U.S. Patent 4,081,561 Meyer et al relates to a process of producing partially decaffeinated soluble coffee. At numerous stages in the Meyer et al process an aqueous extract, which may be dilute or relatively concentrated, exists; such aqueous extracts can be processed per the present- invention to remove glyco
  • Patent 4,088,794 Katz et al is an improve ⁇ ment upon classical coffee extraction processes which are semi-continuous, counter-current extractions of soluble coffee solids from roasted and ground coffee using an aqueous extraction liquid, Katz et al per- forming extraction at a specified liquid velocity in a first stage extraction column of at least 0.50 ft/min; extracts as are obtained in Katz et al can be pro ⁇ Ded per the present invention to remove glyco ⁇ protein therefrom.
  • U.S. Patent 4,092,436 MacDonald et al analyzes in detail various considerations involved in "pre- wetting" a charge of roast, ground coffee to, inter ft]
  • OMPI alia, eliminate the problem of excessive pressure drops in both steam and aqueous extraction operations.
  • the product of an aqueous extraction as performed in MacDonald et al can be subjected to processing per the present invention to remove glycoprotein therefor .
  • U.S. Patent 4,100,306 Gregg et al discloses a method of making an improved soluble coffee compris ⁇ ing, inter alia, one or more procedural steps which result in the obtaining of a volatiles-laden extract and an aqueous coffee extract; the volatiles-laden extract is formed by contacting a frost with at least an equal weight of aqueous coffee extract; aqueous coffee extracts or aqueous systems containing the same obtained following the procedure of Gregg et al can be processed per the present invention to remove glyco ⁇ protein therefrom.
  • U.S. Patent 4,129,665 Clark relates to improve ⁇ ments on the classical liquid extraction process used with roast, ground coffee.
  • the process of the present invention can be applied to liquid extracts obtained per the teaching of Clark to remove glycoprotein therefrom.
  • the present invention also finds application in the formation of chocolate and cocoa of reduced allergenicity and thrombogenicity. While many processes relating to the formation of chocolate and cocoa do not necessarily involve an aqueous extrac ⁇ tion, the present invention modifies the same by including an aqueous extraction step which is followed by, or substantially simultaneous with, glycoprotein precipitation.
  • U.S. Patent 3,997,680 Chalin dis ⁇ closes a method of dutching cocoa; the process of Chalin can be modified so that when the intermediates of Chalin are contacted with an aqueous solution, sufficient aqueous solution is utilized to extract glycoprotein therefrom, the supernanent is withdrawn and glycoprotein precipitated therefrom, whereafter, if desired, the supernanent is returned to the initial precipitate.
  • U.S. Patent 4,078,093 Girsh discloses hypoaller- genic chocolate; Girsh differs substantially from the present invention in involving the use of a heat treatment which denatures substantially all protein allergens which cause chocolate allergies.
  • the glyco- protein of the present invention is, however, heat- resistant and if processed at the conditions of Girsh, would not be denatured.
  • the present invention is thus based upon a discovery substantially different from that of Girsh.
  • certain individuals are genetically predisposed to allergic reaction upon contact with substances which do not produce any such responses in normal people. These substances comprise a particular class of antigens, or substances capable of provoking an immune response, called "allergens.”
  • allergens elicit the production of immunoglo- bulin proteins in genetically predisposed or "atopic" individuals, which proteins in turn mediate a number of clinical disorders, including allergic asthma, aUergenic rhinitis (hay-fever) and urticaria (hives). .
  • All immunoglobulin proteins are composed of similar basic structural units, each subunit having four polypeptides chains which themselves are distin ⁇ guishable into two groups, depending upon molecular weight.
  • the polypeptide chains with molecular weight of about 50,000 are denoted "heavy-chains” or H-chains, while chains with molecular weight of ap ⁇ proximately 20,000 are "light-chains" or L-chains.
  • immunoglobulins The ability of immunoglobulins to function as antibodies in response to specific antigenie stimuli resides in the H-chain constituent of the immunoglobu ⁇ lin molecule. Five different types of been recognized, and together they define the anti- genic classes to which all immunoglobulin molecules belong. Thus, an immunoglobulin protein can be clas ⁇ sified as either an IgA, IgD, IgE, IgG or IgM, depend- ing on the type of H-chain it carries. In addition, refined antigenic analysis of human immunoglobulins can distinguish four sub-types of IgG, two sub-types of IgA, and two sub-types of IgM.
  • immuno ⁇ globulin antibodies of the IgE class and of the IgG 4 class, or "reagins,” are produced.
  • Such reaginic antibodies display affinity for the plasma membrane of mast-cells, blood neutrophiles and blood basophiles.
  • Cells which bind the reagins can become sensitized to the allergens which induced the production of the Ig antibodies.
  • Cells that are sensitized in this fashion will rupture and undergo degranulation im ⁇ mediately upon subsequent contact with the allergen, the result being the release from the degranulating cells of one or more vasoactive mediator substances, such as histamine, or precursors, thereof.
  • the re ⁇ lease of such a mediator substance by reagin- sensitized cells upon contact with allergens is be- lieved to underlie many atopic responses in hyper ⁇ sensitive individuals.
  • histamine is a common vasoactive mediator substance in atopic individuals
  • antihistaminic drugs can be effective in the treatment of histamine- mediated allergic states.
  • mediators may be important to particular atopic condi ⁇ tions, such as asthma and eczema, antihistamines are generally ineffective in combating such conditions.
  • topical or systemic vasoconstric- tors such as -adrenergic agents, are employed to reverse the physiological action of histamine and other vasoactive mediators on the vasculature of mucousal tissue.
  • topical vasoconstric ⁇ tors taken intranasally as nose drops can be effective in shrinking inflammed nasal mucous, a common symptom of allergic rhinitis.
  • systemic decongestants which act by non-specific vasoconstriction, may effect an increase in systemic blood pressure which is contraindicated in hypertensive patients.
  • topical vasocon- strictors while more specific in their effects, are often habituating and nearly always capable of produc ⁇ ing a "rebound" response, wherein delayed vasodilation follows the initial vasoconstriction.
  • desensitization the patient is serially exposed to minute amounts of an allergen or an allergen-containing extract, with the dosage of each exposure gradually increased over a period ex ⁇ tending several months.
  • the regimen of aUergenic exposures is thought to stimulate the production of IgG (and perhaps IgM and IgA) antibodies reactive with the specific antigen.
  • the antibodies are avail ⁇ able thereafter to react with the antigen before it is bound by the reaginic IgE antibodies.
  • blocking antibodies Such antibodies are referred to as "blocking antibodies” because they block the action of reagins.
  • Conventional desensitization treatments have several drawbacks. First, the effectiveness of the desensitization treatment is critically dependent upon using the antigen or antigens responsible for the allergic symptoms. However, selection of the appro- priate antigens in this context can be difficult, and it may not be possible to isolate in relatively purified form the antigen or antigens of interest. Consequently, the only desensitizing material avail ⁇ able is often an extract containing the desired antigen(s) in unknown, often highly diluted concentra- tions in a mixture with other, unspecified allergic factors also of unknown concentration.
  • One object of the present invention is to provide food products of reduced aUergenic and thrombogenic characteristics obtained by removing certain aller- genie and thrombogenic water-soluble glycoproteins therefrom, and a method for obtaining the same.
  • the present invention finds particular application with coffee an ' d cocoa-type products, most especially in the production of soluble coffee of reduced aUergenic and thrombogenic activity.
  • Another object of this invention is to provide a new group of glycoprotein allergens that may be advan ⁇ tageously employed in desensitizing atopic individuals. Yet a further object of this invention to provide a desensitization treatment method with improved effectiveness against a broader range of aUergenic substances.
  • glycoproteins which are functionally similar to TGP have been isolated from coffee and chocolate and from ragweed pollen, and have been shown to be immuno- logically cross-reactive with TGP in experimental animals. It is reasonable to expect that these anti ⁇ genes, like TGP, would also trigger a high incidence of hypersensivity reactions in humans.
  • glycoproteins hereafter often merely “glycoprotein” for brevity
  • polyphenol haptens which activate the factor XII (Hageman factor) dependent pathways of coagulation, fibrinolysis, and kinin generation in normal human plasma.
  • factor XII Heman factor
  • the one or more glycoproteins found to exhibit the above potentially harmful effects are water- soluble, have a molecular weight of about 18,000 to about 40,000 daltons, carry one or more haptens which activate factor XII dependent pathways in normal human plasma, have an isoelectric point of about 4 to about 5.8 and precipitate from aqueous solution at a pH of about 4.5 to about 4.0.
  • glyco-protein includes the one or more glycoproteins removed per the present invention, fragments thereof removed per the present invention and attached polyphenol haptens removed per the pres ⁇ ent invention, albeit results to date indicate the fragments or polyphenol haptens are only thrombogenic.
  • the glycoprotein is highly aUergenic and throm ⁇ bogenic and can be characterized as an antigen or allergen, and can be positively characterized by a number of test procedures,- later described in detail, which can be summarized as follows: (1) Activation of factor XII dependent pathways in normal human plasma, including coagulation, fibrin- olysis and kinin generation as described by Becker, C.G., and T. Dubin, "Cross reactivity and factor XII activation by tobacco, ragweed, and chocolate aller- gens," Circulation 60(4): 11-272 (1979);
  • the present invention is generally applicable to removing glycoprotein from food products where the food products are amenable to aqueous extraction of the glycoprotein.
  • the present invention finds most particular application in removing glyco ⁇ protein from soluble coffee, i.e., instant coffee, since glycoprotein occurs therein in substantial amounts and commercial processings used to form solu- ble coffee are easily modified to include the pro ⁇ cessing of the present invention without excess capi ⁇ tal investment.
  • the present invention can be applied to remove glycoprotein from chocolate and cocoa products, albeit typically with some additional capital investment, since many processes for forming chocolate or cocoa do not generally involve a water extraction step like that employed in many commercial methods for obtaining soluble coffee.
  • U.S. Patent 3,778,519 Taralli et al relates to the manu ⁇ facture of cocoa wherein one step involves treatment
  • U.S. Patent 3,754,928 Haney relates to a process for the preparation of dutched cocoa. An alkali treatment is involved and the Haney process could be easily modified to include the glyco ⁇ protein removal of the present invention.
  • the process of the present invention can be applied to food substrates in general which contain glycoprotein; however, since the present invention finds most parti ⁇ cular application in removing glycoprotein from coffee and cocoa, hereafter for illustrative purposes the present invention will be discussed in terms of such removal.
  • the present invention can be applied to any aqueous system which results from extraction of the glycoprotein from a food substrate.
  • aqueous mixtures may be difficult to process effectively, it is preferred in accordance with the present invention that the aqueous system which is processed to remove glycoprotein therefrom be a solution or a very dilute mixture, and most typi- cally a solution is involved wherein glycoprotein and other soluble constituents are present.
  • an aqueous solution more par ⁇ ticularly an aqueous coffee extract, is generally discussed.
  • glycoprotein is precipitated in accordance with the present invention by isoelectric precipitation, in- volving reducing the pH of the aqueous coffee extract to a pH in the range of about 4.5 to about 4.0. It has been found that when the pH is reduced to this range the glycoprotein will precipitate, but precipi ⁇ tation of other desirable factors does not appear to occur, based on results to date.
  • the resulting glycoprotein precipitate can be removed by conventional means, for example, centri- fuging, filtration, and the like, all of which can be practiced in a conventional manner for precipitate removal.
  • the remaining supematent free of glyco- protein thereafter can be subjected to conventional processing steps, for example, freeze drying, spray drying or the like, whereby the soluble coffee product is obtained.
  • a first separation is performed from a foodstuff to attain a foodstuff residue and a supernanant, which supernatant is sub ⁇ jected to glycoprotein removal per the present inven ⁇ tion; after separation of the glycoprotein precipi ⁇ tate, the supernatant can be recycled to the foodstuff residue in those instances where, for example, the supematent from which glycoprotein has been removed contains desirable texturing or flavor components.
  • the present invention thus is predicated upon two points: first, the recognition of the presence of aUergenic and thrombogenic glycoprotein in food substrates, as typified by coffee and cocoa beans; second, the discovery that the glycoprotein can be removed therefrom to provide a product of reduced allergenicity and reduced thrombogenicity.
  • cocoa can be produced by a number of processes, with one typical process being the well- known dutching process.
  • this process after roasting the beans and removing the husk or shell, the remaining pieces of cocoa beans, commonly referred to as nibs, are crushed or ground to break the cells and form a smooth, creamy paste known as a chocolate liquor.
  • the liquor is typically fed to a hydraulic press where a press cake is formed by removing a part of the fat or cocoa butter.
  • the press cake then can be broken and mixed with an alkalizing solution in a pressure cooker and, after vacuum drying, the result- ing cooled product is ground to a fine powder which can be used in various chocolate products.
  • glycoprotein can be extracted at an alkaline pH from the supernanant which results, the supernatant being removed, the pH being reduced to a pH on the order of about 4.5 to 4.0 using any common acid, for example, hydrochloric acid, the glycoprotein precipitated and removed by means as earlier described, and then, if desired, the super ⁇ nanant returned to the original cocoa precipitate. Thereafter, processing is in a conventional fashion except, of course, the cocoa is free of the glyco ⁇ protein described herein.
  • the extraction conditions used to obtain an aqueous system containing the glyco ⁇ protein which is subjected to the glycoprotein removal of the present invention are generally in accordance with prior art procedures as earlier exemplified for forming, e.g., coffee extracts, cocoa extracts and the like, since the glycoprotein removal of the present invention is, for economic reasons, merely introduced as a unique processing step in conventional foodstuff preparation procedures.
  • Foodstuff extraction should not in most instances occur at a pH below about 4.5 since, in this instance, glycoprotein precipitation would be initiated and possibly glycoprotein would undesirably be retained in solid constituents which might be desirable for inclusion in the end product foodstuff.
  • glycoprotein removal step of the present invention finds particular application in the processing of foodstuffs which are extracted to yield a liquid extract of a neutral or alkaline pH, most preferably a pH on the order of 8.5 or above.
  • processing conditions of the present inven ⁇ tion are not overly critical and can be freely varied by one skilled in the art.
  • processing pressure seems to be relatively unimportant, with processing typically being at normal atmospheric pressure.
  • processing cannot be at sub- or super-atmospheric pressures, though results to date indicate that no benefits accompany processing at other than atmo ⁇ spheric pressure.
  • OMPI extraction of glycoprotein is also effective at higher temperatures, for example, temperatures up to the boiling point of the aqueous system being used. Again, however, there is no prohibition against pro- ces ⁇ ing at lower temperatures or processing at temper ⁇ atures up to and including the boiling point of the system, although no substantial benefits apparently are obtained in improving glycoprotein removal by processing at sub- or super-ambient temperatures.
  • the time of processing is also not overly impor ⁇ tant, since results to date indicate that glycoprotein precipitates substantially instantaneously once the requisite pH is reached, i.e., at a pH on the order of about 4.5 to about 4.0. In this regard, as the acid is added glycoprotein immediately becomes visible as a cloudy precipitate in the system.
  • the amount of water used to form an aqueous system is, in a similar fashion, not overly important, albeit sufficient water should be used to ensure adequate removal of glycoprotein from the food sub ⁇ strate being processed; such amounts can easily be selected by one skilled in the extraction art.
  • a glycoprotein has also been extracted from tobacco leaves which has been found to elicit immedi ⁇ ate cutaneous hypersensitivity in certain human sub ⁇ jects.
  • This "tobacco glycoprotein" (TGP) when in- jected intracutaneously, resulted in the immediate development of wheal and flare reactions, indicative of cutaneous hypersensitivity, in a substantial number of human subjects. See Becker, C.G., et al., Proc. Natl. Acad. Sci. USA, loc. cit. (1976).
  • TGP apparently activates the humoral immunologi- cal system by triggering a specific, immunoglobulin- mediated release of histamine or other inflammatory mediators which induce myocardial arrythmias, as described by Levi, R, et al., "Cardiac and pulmonary anaphylaxis induced by tobacco glycoprotein (TGP),” Fed. Proc. 37(3): 590 (1978), and which may induce arteriosclerosis in hypersensitive individuals. See Becker, C.G. and T. Dubin, "Tobacco allergy and car ⁇ diovascular disease," Cardiovascular Medicine 3(8): 851 (1978).
  • TGP has been shown to acti- vate clotting factor XII in human plasma, resulting in the generation of clotting, fibrinolysis and kinin activity. See Becker, C.G. and T. Dubin, J. Exp. Med., loc. cit. (1977).
  • TGP thus can be employed to counter atopic symptoms elicited by aUergenic substances wholly unrelated to tobacco without the problems
  • the present invention there ⁇ fore provides a method of desensitizing individuals to a wide class of allergens, which is predicated broadly upon the discovery that individuals sensitive to, for example, TGP, ragweed, GP-Cof, GP-Coc, etc., can be densensitized to this entire class of allergens by appropriate treatement with merely only one member of the class.
  • a sensitive individual is desensitized to this class of allergens by treatment with GP-Cof and/or GP-Coc
  • individuals sensitive to GP-Cof and/or GP-Coc and/or ragweed pollen are desensitized thereto by treatment with TGP.
  • Example 1 This example illustrates not only the extraction of the glycoprotein from coffee but the further puri ⁇ fication and testing of the glycoprotein.
  • Initial extraction of coffee antigen from Chock- Full O'Nuts Coffee (Candler Coffee Corp., N.Y.C.) was performed with a West Bend coffee machine (West Bend Co., West Bend, Wis.) according to the manufacturer's instruction for preparing coffee.
  • the above procedure is equivalent to a typical extraction as is used in the commercial production of soluble (instant) coffee.
  • the coffee was clarified by centrifugation at 20,000 x g and extracted twice with equal volumes of petroleum ether.
  • the infranate was then extracted twice with equal volumes of ethyl ether, whereby hydrocarbon-soluble components in the coffee were removed. This step is only necessary where one de ⁇ sires to purify the glycoprotein itself, and initial clarification and hydrocarbon extraction are not necessary where the objective is merely to remove the glycoprotein.
  • glycoprotein was then further purified as follows. Isoelectric precipitation of the glyco ⁇ protein from PBS using HCl as above described (pH 4.0-4.5) was repeated three to four times until the supernate was essentially colorless. The final
  • OMPI precipitate was dissolved in 3 ml of PBS and applied to a 2.5 x 100 cm column of Biogel P-10 equilibrated with PBS and then washed with PBS. The brown, void volume peak was collected. The glycoprotein was then concentrated by isoelectric precipitation at pH 4.0 with HCl as above described. The precipitate was collected by centrifugation and redissolved in Tris- barbital buffer at pH 8.9 and applied to an alkaline polyacrylamide gel column, and preparative continuous flow electrophoresis was performed as described by Becker, et al., Proc. Natl. Acad. Sci. USA, loc. cit. (1976). The glycoprotein emerged as a sharp, highly anodic peak.
  • Tubes containing the 20,000-40,000 molecular weight material were pooled, dialyzed exhaustively against distilled water and lyophylized in a conven- tional manner.
  • Example 3 Ragweed pollen was obtained from Greer Labora- tories, Lenoir, N.C. The pollen was pulverized and the glycoprotein extracted therefrom as described in Example 1.
  • glycoproteins hereinafter referred to respectively as GP-Cof (Example 1), GP-Coc (Exam- pie 2), and GP-RW (Example 3), were then tested per the following procedure, along with TGP isolated and purified from tobacco leaf according to the protocol of Becker, et al., Proc. Natl. Acad. Sci. USA, loc. cit. (1976).
  • Glycoprotein Quantification was then tested per the following procedure, along with TGP isolated and purified from tobacco leaf according to the protocol of Becker, et al., Proc. Natl. Acad. Sci. USA, loc. cit. (1976).
  • Electrophoretic/Isoelectric Focusing Analysis TGP, GP-Cof, GP-Coc and antigens from ragweed pollen (GP-RW) were then compared by electrophoresis and isoelectric focusing.
  • OMPI TGP, GP-Cof, GP-Coc and RW were compared by electrophoresis on alkaline 7.5% polyacrylamide gels according to the method of Davis and Ornstein, de ⁇ scribed in Methods in Immunology and Immunochemistry, Vol. II, CA. Williams and M.W. Chase (eds.). Academic Press (N.Y. ), 1968, pages 38-47. Following electro ⁇ phoresis the gels were fixed in methanol: acetic acid: water (40:10:50:) and stained with either Coomassie Brilliant Blue or the PAS reaction.
  • TGP, GP-Cof, GP-Coc and RW were found to migrate identically in alkaline 7.5% polyacrylamide gels re- suiting in bands which were PAS positive and (un ⁇ stained) providing gels which were brown - GP-Cof, red-brown - GP-Coc or yellow-brown - RW.
  • Euglobulin Clot Lysis Time The effect of these antigens on euglobulin clot lysis time (ECLT) was mea- sured according to the technique of Ogston D., et al., "The assay of a plasma component necessary for the generation of a plasminogen activator in the presence of Hageman factor (Hageman co-factor)," Brit. J. Haematol.20:209 (1971).
  • Kallikrein Activity - Normal citrated plasma which had been stored at -70°C was activated at 37°C for 15 minutes with the glycoproteins in concentra ⁇ tions of approximately 200 ⁇ g/ml plasma.
  • OM ⁇ TGP, GP-Cof, GP-Coc and GP-RW were all capable of shortening the partial thromboplastin (PTT) and euglo ⁇ bulin clot lysis time (ECLT) of normal human plasma.
  • PTT partial thromboplastin
  • ECLT euglo ⁇ bulin clot lysis time
  • TGP was isolated and purified according to the protocol of
  • Control sites were injected wth normal guinea pig serum siluted similar- ly. Eighteen hours later the sensitized animals were injected intravenously with 1 ml of a 1.5% solution of Evans Blue dye. The skin sites were challenged by intradermal injection of 1, 5, or 25 ⁇ g of TGP, GP-Coc, GP-Cof, or GP-RW. Thirty minutes later the animals were sacrificed, skinned, and the zones of leakage of Evans Blue measured and photographed.
  • hyposensitizing material could be adminis ⁇ tered by any of the conventional techniques used by trained allergists, e.g., subcutaneous injection.
  • the dosage levels for the hyposensitizing material are ascertained on a case-by-case basis since the clinical responses to exposure, as is well-known in the field of allergy, differs between subjects.
  • the desensitizing process may be followed during treatment by monitoring the subject for decreasing allergic sensitivity.
  • a standard bioassay tech ⁇ nique such as the wheal-and-flare method, or by quantifying the production- of antibodies of different classes using, e.g., a radioimmunoassay technique.

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PCT/US1981/001353 1980-10-08 1981-10-07 Lower allergenicity and lower thrombogenicity foodstuff and process for preparing the same WO1982001132A1 (en)

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DE19813152395 DE3152395A1 (de) 1980-10-08 1981-10-07 Nahrungsmittel mit niedriger allergenitaet und niedriger thrombogenitaet und verfahren zu dessen herstellung

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Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE3800323A1 (de) * 1988-01-08 1989-07-20 Jacobs Suchard Ag Hypoallergenische schokolade
US5328991A (en) * 1989-11-03 1994-07-12 Immulogic Pharmaceutical Corp. Preparation of alkali-modified cat dander allergen (Fel d I) for immunotherapeutic purposes
WO2003013264A1 (en) * 2001-08-01 2003-02-20 Societe Des Produits Nestle S.A. Hypoallergenic chocolate

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN100415292C (zh) * 2000-07-13 2008-09-03 “爱多法姆”生产联合企业股份有限公司 新型生物活性糖蛋白

Citations (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1613313A (en) * 1926-04-03 1927-01-04 Frank A Csonka Product adapted for use in the treatment of hay fever
US2309884A (en) * 1940-05-02 1943-02-02 Bresnick Harry Processing of foods
US2500145A (en) * 1946-02-21 1950-03-14 Patten Pharmaceutical Company Oral pollen antigen and process of preparing same
US3845220A (en) * 1971-10-21 1974-10-29 Ogawa & Co Ltd Coffee carbonated beverage
US3846937A (en) * 1973-03-29 1974-11-12 Univ Minnesota Production of allergens by plant tissue culture technique
US3893993A (en) * 1969-08-06 1975-07-08 Beecham Group Ltd Allergenic extracts cross linked under acid conditions with inorganic cyanates
US3995023A (en) * 1972-12-11 1976-11-30 Merck Patent Gesellschaft Mit Beschrankter Haftung Process for the production of allergen-containing extracts
US4078093A (en) * 1976-10-12 1978-03-07 Girsh Leonard S Hypoallergenic chocolate
US4140679A (en) * 1976-10-12 1979-02-20 Research Corporation Antigen-protein complex for blocking allergic reactions
US4208440A (en) * 1978-05-22 1980-06-17 Schmidt Edward D Electrically separating a food paste
US4269764A (en) * 1979-08-02 1981-05-26 Roy Patterson Preparation for treatment of allergic patients sensitive to ragweed pollen

Patent Citations (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1613313A (en) * 1926-04-03 1927-01-04 Frank A Csonka Product adapted for use in the treatment of hay fever
US2309884A (en) * 1940-05-02 1943-02-02 Bresnick Harry Processing of foods
US2500145A (en) * 1946-02-21 1950-03-14 Patten Pharmaceutical Company Oral pollen antigen and process of preparing same
US3893993A (en) * 1969-08-06 1975-07-08 Beecham Group Ltd Allergenic extracts cross linked under acid conditions with inorganic cyanates
US3845220A (en) * 1971-10-21 1974-10-29 Ogawa & Co Ltd Coffee carbonated beverage
US3995023A (en) * 1972-12-11 1976-11-30 Merck Patent Gesellschaft Mit Beschrankter Haftung Process for the production of allergen-containing extracts
US3846937A (en) * 1973-03-29 1974-11-12 Univ Minnesota Production of allergens by plant tissue culture technique
US4078093A (en) * 1976-10-12 1978-03-07 Girsh Leonard S Hypoallergenic chocolate
US4140679A (en) * 1976-10-12 1979-02-20 Research Corporation Antigen-protein complex for blocking allergic reactions
US4208440A (en) * 1978-05-22 1980-06-17 Schmidt Edward D Electrically separating a food paste
US4269764A (en) * 1979-08-02 1981-05-26 Roy Patterson Preparation for treatment of allergic patients sensitive to ragweed pollen

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
COFFEE PROCESSING TECHNOLOGY, VOLUME 2, PUBLISHED 1963, PUBLISHED BY AVI PUBLISHING COMPANY, WESTPORT, CONNECTICUT, PAGES 120,121,163,164,165 *
INTRODUCTION TO CLINICAL ALLERGY, PUBLISHED 1973, PUBLISHED BY CHARLES C. THOMAS: SPRINGFIELD, OHIO, PAGES 290,297 *
NATIONAL ACADEMY OF SCIENCE PROCEEDINGS, VOLUME 73, ISSUED MAY 1976, WASHINGTON, D.C., C.G. BECKER, HYPERSENSITIVITY TO TOBACCO ANTIGEN, PP. 1712-1716 *
THE JOURNAL OF EXPERIMENTAL MEDICINE, VOLUME 146, ISSUED 1977, NEW YORK, C.G. BECKER, ACTIVATION OF FACTOR XII BY TOBACCO GLYCOPROTEIN, PP. 457-467 *

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE3800323A1 (de) * 1988-01-08 1989-07-20 Jacobs Suchard Ag Hypoallergenische schokolade
US4963372A (en) * 1988-01-08 1990-10-16 Jacobs Suchard Ag Consumer friendly chocolate
US5328991A (en) * 1989-11-03 1994-07-12 Immulogic Pharmaceutical Corp. Preparation of alkali-modified cat dander allergen (Fel d I) for immunotherapeutic purposes
WO2003013264A1 (en) * 2001-08-01 2003-02-20 Societe Des Produits Nestle S.A. Hypoallergenic chocolate

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