NO761306L - - Google Patents
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- Publication number
- NO761306L NO761306L NO761306A NO761306A NO761306L NO 761306 L NO761306 L NO 761306L NO 761306 A NO761306 A NO 761306A NO 761306 A NO761306 A NO 761306A NO 761306 L NO761306 L NO 761306L
- Authority
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- Prior art keywords
- glycoprotein
- pregnancy
- specific
- solution
- value
- Prior art date
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-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4715—Pregnancy proteins, e.g. placenta proteins, alpha-feto-protein, pregnancy specific beta glycoprotein
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
- G01N33/76—Human chorionic gonadotropin including luteinising hormone, follicle stimulating hormone, thyroid stimulating hormone or their receptors
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Urology & Nephrology (AREA)
- Endocrinology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Reproductive Health (AREA)
- Analytical Chemistry (AREA)
- Pregnancy & Childbirth (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Physics & Mathematics (AREA)
- Biotechnology (AREA)
- Food Science & Technology (AREA)
- Cell Biology (AREA)
- Gynecology & Obstetrics (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Description
Fremgangsmåte til anrikning avMethod for the enrichment of
' svangerskaps spes i fikt $-^-glykoprot ein,' pregnancy spes in fict $-^-glycoprot ein,
I tysk søknad 21 57 610 er det omtalt et i plazenta forekommende glykoprotein, som tilkommer betegnelsen "svangerskapsspesifikt B-^-glykoprotein" (SP1) . Videre er det i nevnte søknad omtalt en fremgangsmåte til isolering av dette glykoprotein. In German application 21 57 610, a glycoprotein occurring in the placenta is mentioned, which is called "pregnancy-specific B-^-glycoprotein" (SP1). Furthermore, the aforementioned application describes a method for isolating this glycoprotein.
Det er nå funnet en fremgangsmåte som muliggjør isolering av det svangerskapsspesifikke gn-glykoprotein i bedre utbytte og .større renhet. Fremgangsmåten erkarakterisert vedat man bringer blodserum, urin eller plazentaekstrakt ved en pH-verdi mellom 4 og 9 i berøring med et til en uoppløse-lig bærer bundet antilegeme mot svangerskapsspesif ikt 3-|_-glykoprotein, adskiller bæreren som inneholder glykoproteinet bundet, fra den flytende fase og ti-1 utløsning av glykoproteinet behandler med et vandig medium av pH-verdi 2-4 eller en oppløs-ning av et stoff som dissosierer proteinmolekyler ved en pH-verdi på 4 - 9, fortrinnsvis ca. pH 7- A method has now been found which enables the isolation of the pregnancy-specific gn-glycoprotein in better yield and greater purity. The method is characterized by bringing blood serum, urine or placenta extract at a pH value between 4 and 9 into contact with an antibody bound to an insoluble carrier against pregnancy-specific 3-|_-glycoprotein, separating the carrier containing the bound glycoprotein from the liquid phase and ti-1 release of the glycoprotein treated with an aqueous medium of pH value 2-4 or a solution of a substance that dissociates protein molecules at a pH value of 4-9, preferably approx. pH 7-
Ved denne fremgangsmåte fremstilles det svangerskapsspesif ikke 3-^-glykoprotein fra disse oppløsninger ved spesifikk immunadsorpsjon ved hjelp av en bærer, som inneholder det tilsvarende antilegeme i uoppløselig form. In this method, pregnancy-specific non-3-β-glycoprotein is produced from these solutions by specific immunoadsorption with the aid of a carrier, which contains the corresponding antibody in insoluble form.
Antilegemet som på kjent måte kan bindes til en fast bærer fåes ved immunisering av dyr med det svangerskapsspesifikke 3-]_-glykoprotein. Blodet fra således behandlede for-søksdyr opparbeides på kjent måte til fremstilling av immuno-globulinf raks j onen. Det på denne måte dannede anti-SP]_-serum bindes til tilsvarende kjente fremgangsmåter til egnet bærer. Slike fremgangsmåter er eksempelvis omtalt i Ann. Rev. Biochem. 40 (1971) 259; Naturwissenschaften 58 (1971) 389 eller Nature 214 (1967) 1302. Spesielt egnede bærer er høypolymere kullhydrater som cellulose eller agar, syntetiske harpikser som polyakrylamid eller kopolymere av etylen/maleinsyreanhydrid. The antibody, which can be bound to a solid carrier in a known manner, is obtained by immunizing animals with the pregnancy-specific 3-]_-glycoprotein. The blood from experimental animals treated in this way is processed in a known manner to produce the immunoglobulin fraction. The anti-SP]_ serum formed in this way is bound to a suitable carrier by similar known methods. Such methods are described, for example, in Ann. Fox. Biochem. 40 (1971) 259; Naturwissenschaften 58 (1971) 389 or Nature 214 (1967) 1302. Particularly suitable carriers are high polymer carbohydrates such as cellulose or agar, synthetic resins such as polyacrylamide or copolymers of ethylene/maleic anhydride.
Også glasspartikler kan anvendes som bærere.Glass particles can also be used as carriers.
Spesielt foretrukket som bærematerial er en renset agarose i form av små kuler med en diameter på ca. 20 - 200^um, hvortil etter den ovenfor sistnevnte metode anti-legemene kan bindes kovalent mot SP-^. Especially preferred as carrier material is a purified agarose in the form of small spheres with a diameter of approx. 20 - 200 μm, to which, according to the above-mentioned method, the antibodies can be covalently bound to SP-^.
Por isolering av SP^fra oppløsninger som des-suten inneholder andre proteiner og kullhydrater som plazenta-ekstrakter eller serum eller urin fra svangere, bringes de nevnte utgangsstoffer i berøring med adsorbenset som bærer antilegemet, idet pH-verdien innstilles på over 4. Por å unngå en denaturering av proteinet lønner dét seg å velge pHrverdien ikke høyere enn 9- Saltkonsentrasjonen av oppløsningen er ikke kritisk. Imidlertid bør det unngås betingelser som er egnet til å løse bindingen av antigenet til antilegemet. Fortrinnsvis inneholder den vandige oppløsning nøytrale salter og/eller pufferstoffer slik de vanligvis anvendes i biokjemiske reak-sjoner, spesielt natriumklorid, fosfatpuffere, trishydroksy-metylaminometan eller andre kjente pufferstoffer, slik de eksempelvis er omtalt i Biochemistry 5 (1966) 472. Konsentrasjonen av disse stoffer ligger hensiktsmessig i området mellom 0,01 og 2 mol/liter. Forholdet proteinoppløsning : adsorbens er hensiktsmessig i området 1 : 1 til 10 : 1, fortrinnsvis : 1. Adsorbenset bør forbli i berøring med proteinoppløsningen For the isolation of SP^ from solutions which also contain other proteins and carbohydrates such as placental extracts or serum or urine from pregnant women, the aforementioned starting substances are brought into contact with the adsorbent carrying the antibody, the pH value being set above 4. avoid a denaturation of the protein, it pays to choose a pH value no higher than 9 - The salt concentration of the solution is not critical. However, conditions suitable to dissolve the binding of the antigen to the antibody should be avoided. Preferably, the aqueous solution contains neutral salts and/or buffer substances as they are usually used in biochemical reactions, in particular sodium chloride, phosphate buffers, trishydroxymethylaminomethane or other known buffer substances, as for example described in Biochemistry 5 (1966) 472. The concentration of these substances are suitably in the range between 0.01 and 2 mol/litre. The ratio protein solution : adsorbent is appropriate in the range 1 : 1 to 10 : 1, preferably : 1. The adsorbent should remain in contact with the protein solution
0,1 til 5 timer for at det skal stå tilstrekkelig tid til dis-posisjon til å.knytte antigen-antilegemebindingen. 0.1 to 5 hours in order to allow sufficient time for dis-position to form the antigen-antibody bond.
Adsorbenset adskilles deretter fra oppløsningenThe adsorbent is then separated from the solution
ved sentrifugering eller filtrering og vaskes flere ganger med en nøytral saltoppløsning for å eliminere overskytende salter og uspesifikt adsorberte forurensninger. by centrifugation or filtration and washed several times with a neutral salt solution to eliminate excess salts and non-specifically adsorbed contaminants.
Elueringen av SP-^fra antilegemeholdige bærereThe elution of SP-^ from antibody-containing carriers
kan foregå på kjent måte ved forholdsregler som bevirker oppløs-ning av antigen-antilegeme-bindingen. Eksempelvis kan elueringen foregå ved innbringning av bæreren i et vandig medium på pH-verdi under 4, fortrinnsvis mellom 2 og 4. Den tilsvarende oppløsning bør inneholde salter av egnede pufferstoffer i egnet konsentrasjon, fortrinnsvis 0,2 til 8 mol pr. liter. can take place in a known manner by precautions which cause the antigen-antibody bond to dissolve. For example, the elution can take place by introducing the carrier into an aqueous medium with a pH value below 4, preferably between 2 and 4. The corresponding solution should contain salts of suitable buffer substances in a suitable concentration, preferably 0.2 to 8 mol per litres.
Det lønne.r seg å omrøre dispersjonen av adsorbenset i denne oppløsning 0,1 til 2 timer, idet SP-^desorberes av immunadsorbenset. Etter adskillelse av adsorbens innstilles pH-verdien av den SP-^-holdige oppløsning til ca. nøytral (6 til 8). Oppløsningen kan hvis ønsket underkastes en ytterligere rensning, eksempelvis fra adsorpsjon på hydroksylapatit. It pays to stir the dispersion of the adsorbent in this solution for 0.1 to 2 hours, as the SP is desorbed by the immunoadsorbent. After separation of adsorbent, the pH value of the SP-^-containing solution is adjusted to approx. neutral (6 to 8). If desired, the solution can be subjected to further purification, for example from adsorption on hydroxylapatite.
Elueringen av SP-^fra den antilegeme-holdige bærer kan også foregå ved hjelp av proteindissosierende stoffer, eksempelvis urinstoffoppløsninger eller oppløsninger av såkalte kaotrope salter som NaNO^, NaBr, NaClO^, CF^COONa, NaSCN eller CCl-^COONa. Konsentrasjonen av disse salter i elueringsmediet utgjør hensiktsmessig 0,2 til 8 mol/liter. Por å fjerne protein-molekyldissosierende stoffer fra. oppløsningen etter desorpsjonen av SPjog til adskillelse av adsorbenset kan oppløsningen dialyseres mot en nøytralsaltoppløsning eller pufferoppløsningen av konsentrasjon 0,1 til 1 mol/liter. The elution of SP-^ from the antibody-containing carrier can also take place with the help of protein-dissociating substances, for example urea solutions or solutions of so-called chaotropic salts such as NaNO^, NaBr, NaClO^, CF^COONa, NaSCN or CCl-^COONa. The concentration of these salts in the elution medium is suitably 0.2 to 8 mol/litre. Por to remove protein-molecule dissociating substances from. the solution after the desorption of SP and to separate the adsorbent, the solution can be dialyzed against a neutral salt solution or the buffer solution of concentration 0.1 to 1 mol/litre.
Det etter denne fremgangsmåte dannede SP-^ har en renhetsgrad fra 60 til 95%- Ved ytterligere rensningsfrem-gangsmåter kan det anrikes til over 99%. The SP-^ formed by this method has a degree of purity of from 60 to 95% - With further purification methods, it can be enriched to over 99%.
Fremgangsmåten skal forklares nærmere ved hjelpThe procedure must be explained in more detail with help
av et eksempel:of an example:
Eksempel.Example.
Isolering av svangerskapsspesifikt 3-|_-glykoprotein fra dets oppløsninger ved immunadsorps j on. . Et til spesifikk binding av svangerskapsspesifikt 3-£~glykoprotein egnet immunoadsorbens får man ved kovalent sammenknytning av anti-svangerskapsspesifikt 3-^-glykoprotein-immunoglobuliner med en egnet bærer. Det i foreliggende eksempel anvendte immunoadsorbens ble fremstillet ved binding av 1,75 g protein av en fra anti-svangerskapsspesif ikt 8-^-glykoprotein-kaninserum utvunnet immunoglobulinfraksjon på 175 g "Sepharose 4 B" (Pharmacia Uppsala), som var blitt aktivert med 21,8 g BrCN, (Axen, R., Porath, J., Ernbach, S.: Nature 214, 1302 (1967))- Ved hjelp av denne immunoadsorbens lar det seg isolere svangerskapsspesif ikt 3-^-glykoprotein etter følgende fremgangsmåte fra ekstraktet fra plazenta: Det svangerskapsspesifikke Sj-glykoproteinholdig plazentaekstrakt dialyseres i første rekke mot 0,1 molar tris-hydroksymetylaminometan-saltsyre-puffer (pH 8,0), som inneholder 1,0 mol/liter NaCl og 1 g/liter natriumazid. Til denne oppløs-ning har man som spesifikk adsorbens det bærerbundne antisvanger-skapsspesifikke 3-|_-glykoprotein-immunoglobulin, omrører 2 timer ved 4°C og frasuger på en filternutsch adsorbenset med det bundede svangerskapsspesifikke 3^glykoprotein. Adsorbenset vaskes i første rekke med 2 x 250 ml av den 0,1 molare tris- hydroksymetylaminometan-saltsyre-pufferoppløsning og deretter med 2 x 250 ml av en fysiologisk (0,9%-ig) kokesaltoppløsning, deretter eluerer man det svangerskapsspesifikke 3^-glykoprotein fra adsorbenset ved seks gangers behandling av adsorbenset Isolation of pregnancy-specific 3-|_-glycoprotein from its solutions by immunoadsorb ion. . An immunoadsorbent suitable for specific binding of pregnancy-specific 3-β-glycoprotein is obtained by covalently linking anti-pregnancy-specific 3-β-glycoprotein immunoglobulins with a suitable carrier. The immunoadsorbent used in the present example was prepared by binding 1.75 g of protein from an immunoglobulin fraction extracted from anti-pregnancy-specific 8-β-glycoprotein rabbit serum on 175 g of "Sepharose 4 B" (Pharmacia Uppsala), which had been activated with 21.8 g BrCN, (Axen, R., Porath, J., Ernbach, S.: Nature 214, 1302 (1967))- Using this immunoadsorbent, pregnancy-specific 3-^-glycoprotein can be isolated according to the following procedure from the extract from the placenta: The pregnancy-specific Sj-glycoprotein-containing placental extract is first dialysed against 0.1 molar tris-hydroxymethylaminomethane-hydrochloric acid buffer (pH 8.0), which contains 1.0 mol/liter NaCl and 1 g/liter sodium azide. For this solution, the specific adsorbent is the carrier-bound anti-pregnancy-specific 3-|_-glycoprotein immunoglobulin, stirred for 2 hours at 4°C and the adsorbent with the bound pregnancy-specific 3-glycoprotein is sucked off on a filter nut. The adsorbent is first washed with 2 x 250 ml of the 0.1 molar tris-hydroxymethylaminomethane-hydrochloric acid buffer solution and then with 2 x 250 ml of a physiological (0.9% saline solution), then the pregnancy-specific 3^ is eluted -glycoprotein from the adsorbent by treating the adsorbent six times
hver gang 20 minutter med 400 ml av en 0,5 molar glycin-HCl-each time 20 minutes with 400 ml of a 0.5 molar glycine-HCl-
puffer av pH-verdi 2,5- De forenede eluater innstilles med 1 N NaOH på pH 7,0 og inndampes på et ultrafilter til 10 ml. buffer of pH value 2.5 - The combined eluates are adjusted with 1 N NaOH to pH 7.0 and evaporated on an ultrafilter to 10 ml.
Den svangerskapsspesif ikke 3-j_-glykoproteinholdige oppløsningThe pregnancy-specific non-3-j_-glycoprotein-containing solution
gjøres deretter ved dialyse saltfri overfor vann og lyofili-is then made salt-free from water and lyophilic by dialysis
seres til slutt. Hvis ønsket kan vidererensningen av SP-^-oppløsningen f.eks. foretas ved følgende fremgangsmåte. Kon-sentratet dialyseres mot en 0,005 molar natriumfosfatpuffer av pH-verdi 6,8 og/eller vidererenses ved kromatografi på hydroksylapatit. Derved adsorberes de av immunoadsorbenset uspesifikt bundne og deretter eluerte plasmaproteiner til hydroksylapatitten, men gjennomløpet foreligger det svangerskapsspesif ikke B-]_-glykoprotein i høyrenset form. (renhet over 99$). seen in the end. If desired, the further purification of the SP-^ solution can e.g. is carried out by the following procedure. The concentrate is dialysed against a 0.005 molar sodium phosphate buffer of pH 6.8 and/or further purified by chromatography on hydroxylapatite. Thereby, the plasma proteins non-specifically bound by the immunoadsorbent and then eluted are adsorbed to the hydroxylapatite, but the pregnancy-specific non-pregnancy B-]_-glycoprotein is present in a highly purified form. (purity above 99$).
Samme fremgangsmåte kan anvendes, når det skal fremstilles det svangerskapsspesif ikke (3-^-glykoprotein fra serum eller urin åv svangre. The same procedure can be used when the pregnancy-specific (3-^-glycoprotein from serum or urine of pregnant women is to be prepared.
Claims (1)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US05/569,476 US4065445A (en) | 1971-09-29 | 1975-04-18 | Pregnancy-specific β1 -glycoprotein and process for isolating it |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO761306L true NO761306L (en) | 1976-10-19 |
Family
ID=24275609
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO761306A NO761306L (en) | 1975-04-18 | 1976-04-14 | |
| NO761305A NO145405C (en) | 1975-04-18 | 1976-04-14 | PROCEDURE FOR PURIFICATION OF THE PREGNANCY-SPECIFIC BETA-1 GYCLOPROTEIN |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO761305A NO145405C (en) | 1975-04-18 | 1976-04-14 | PROCEDURE FOR PURIFICATION OF THE PREGNANCY-SPECIFIC BETA-1 GYCLOPROTEIN |
Country Status (18)
| Country | Link |
|---|---|
| JP (2) | JPS51133408A (en) |
| AT (2) | AT344920B (en) |
| AU (2) | AU503342B2 (en) |
| BE (2) | BE840913A (en) |
| CA (2) | CA1065305A (en) |
| DE (1) | DE2612479A1 (en) |
| DK (2) | DK173576A (en) |
| ES (2) | ES446939A1 (en) |
| FI (2) | FI54486C (en) |
| FR (2) | FR2307816A1 (en) |
| GB (2) | GB1541454A (en) |
| IE (2) | IE42679B1 (en) |
| IT (1) | IT1060215B (en) |
| LU (2) | LU74782A1 (en) |
| NL (2) | NL7603902A (en) |
| NO (2) | NO761306L (en) |
| NZ (1) | NZ180619A (en) |
| SE (2) | SE7604483L (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2720704C2 (en) * | 1977-05-07 | 1986-09-25 | Behringwerke Ag, 3550 Marburg | New glycoprotein, process for its production and its uses |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5325030B2 (en) * | 1972-12-19 | 1978-07-24 |
-
1976
- 1976-03-24 DE DE19762612479 patent/DE2612479A1/en active Pending
- 1976-04-12 ES ES446939A patent/ES446939A1/en not_active Expired
- 1976-04-12 ES ES446944A patent/ES446944A1/en not_active Expired
- 1976-04-13 NL NL7603902A patent/NL7603902A/en not_active Application Discontinuation
- 1976-04-13 NL NL7603903A patent/NL7603903A/en not_active Application Discontinuation
- 1976-04-14 FI FI761016A patent/FI54486C/en not_active IP Right Cessation
- 1976-04-14 DK DK173576A patent/DK173576A/en active IP Right Grant
- 1976-04-14 NO NO761306A patent/NO761306L/no unknown
- 1976-04-14 FI FI761017A patent/FI56184C/en not_active IP Right Cessation
- 1976-04-14 NO NO761305A patent/NO145405C/en unknown
- 1976-04-14 DK DK173876A patent/DK173876A/en active IP Right Grant
- 1976-04-15 GB GB15558/76A patent/GB1541454A/en not_active Expired
- 1976-04-15 AU AU13082/76A patent/AU503342B2/en not_active Expired
- 1976-04-15 SE SE7604483A patent/SE7604483L/en not_active Application Discontinuation
- 1976-04-15 CA CA250,426A patent/CA1065305A/en not_active Expired
- 1976-04-15 CA CA250,439A patent/CA1065307A/en not_active Expired
- 1976-04-15 SE SE7604484A patent/SE419340B/en unknown
- 1976-04-15 IE IE818/76A patent/IE42679B1/en unknown
- 1976-04-15 GB GB15557/76A patent/GB1541453A/en not_active Expired
- 1976-04-15 NZ NZ180619A patent/NZ180619A/en unknown
- 1976-04-15 AU AU13081/76A patent/AU503288B2/en not_active Expired
- 1976-04-15 IE IE817/76A patent/IE42566B1/en unknown
- 1976-04-16 AT AT284176A patent/AT344920B/en not_active IP Right Cessation
- 1976-04-16 IT IT22445/76A patent/IT1060215B/en active
- 1976-04-16 LU LU74782A patent/LU74782A1/xx unknown
- 1976-04-16 AT AT284276A patent/AT344734B/en not_active IP Right Cessation
- 1976-04-16 FR FR7611372A patent/FR2307816A1/en active Granted
- 1976-04-16 LU LU74783A patent/LU74783A1/xx unknown
- 1976-04-16 FR FR7611367A patent/FR2307815A1/en active Granted
- 1976-04-17 JP JP51044151A patent/JPS51133408A/en active Pending
- 1976-04-17 JP JP51044152A patent/JPS51133406A/en active Granted
- 1976-04-20 BE BE166291A patent/BE840913A/en not_active IP Right Cessation
- 1976-04-20 BE BE166290A patent/BE840912A/en unknown
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