WO1983002123A1 - PROCEDE ET AGENT DE REACTION POUR DETECTER DES ENDOTOXINES OU DES 'beta'-1,3 GLUCANES A PARTIR DE CHAMPIGNONS OU BACTERIES - Google Patents

PROCEDE ET AGENT DE REACTION POUR DETECTER DES ENDOTOXINES OU DES 'beta'-1,3 GLUCANES A PARTIR DE CHAMPIGNONS OU BACTERIES Download PDF

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Publication number
WO1983002123A1
WO1983002123A1 PCT/SE1982/000430 SE8200430W WO8302123A1 WO 1983002123 A1 WO1983002123 A1 WO 1983002123A1 SE 8200430 W SE8200430 W SE 8200430W WO 8302123 A1 WO8302123 A1 WO 8302123A1
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Prior art keywords
arg
pna
gly
astacus
blood cell
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PCT/SE1982/000430
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English (en)
Inventor
Kenneth Tord Soederhaell
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SÖDERHÄLL, Kenneth, Tord
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Priority to JP83500092A priority Critical patent/JPS58502082A/ja
Publication of WO1983002123A1 publication Critical patent/WO1983002123A1/fr

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Classifications

    • 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
    • G01N33/579—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving limulus lysate
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
    • C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
    • C07K5/08—Tripeptides
    • C07K5/0802—Tripeptides with the first amino acid being neutral
    • C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
    • C07K5/0808—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving viable microorganisms
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
    • C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
    • C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
    • C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2400/00—Assays, e.g. immunoassays or enzyme assays, involving carbohydrates
    • G01N2400/10—Polysaccharides, i.e. having more than five saccharide radicals attached to each other by glycosidic linkages; Derivatives thereof, e.g. ethers, esters
    • G01N2400/12—Homoglycans, i.e. polysaccharides having a main chain consisting of one single sugar
    • G01N2400/24—Homoglycans, i.e. polysaccharides having a main chain consisting of one single sugar beta-D-Glucans, i.e. having beta 1,n (n=3,4,6) linkages between saccharide units, e.g. xanthan

Definitions

  • the present invention relates to a method and a reagent for detecting bacterial and fungal infections with a high sensitivity.
  • Various methods for rapidly detecting bacterial infections through Gram-negative bacteria with a relatively high sensitivity are based upon the reaction of a lysate of amebocytes or "blood cells" from horseshoe crabs.
  • the lysate reacts to bacterial endotoxins, which are lipopoiysaccharides, such that gel is formed.
  • This gel phenomenon which is a defense reaction of the horseshoe crab, is elicited by the lipopoiysaccharides activating a serine protease, which in turn converts coagulogen into coagulin.
  • the previous determination methods are based, on one hand, on the gel reaction itself, such as measurement of the gel formation rate, turbidity changes, etc., and, on the other hand, upon the activated serine protease.
  • the last mentioned method which is the definitely most sensitive one and permits detection of conce ⁇ tra tions as low as 10 -6 - 10 -9 mg/ml, utilizes the capability of the serine protease to enzymatically hydrolyze certain synthetically prepared polypeptides, such that specific end groups are cleaved off and thereby form compounds which may be detected colorimetrically or fluorometrically. This method is described in, for example, the German Offenlegungsschrift 2,740,323.
  • a commercial reagent marketed by Kabi Peptide Research Ltd., M ⁇ lndal, Sweden, contains a synthetic peptide having a terminal p-nitroanilide group and a lysate from the American horseshoe crab or Limulus polyphemus. On addition of bacterial lipopoiysaccharides the serine protease of the lysate is activated and the yellow colour of the p-nitroaniline released thereby may be read colorimetrically.
  • coagulogen and at least one serine protease are included in the blood cells of the arthropods crustaceans and insects and are involved in the activation of a coagulation-like reaction in a similar way as in the horseshoe crab, and that therefore both bacterial and fungal infections may be determined qualitatively as well as quantitatively using a blood cell or hemocyte lysate from these animals.
  • a lysate from these arthropods is activated quantitatively by lipopoiysaccharides, or LPS, i.e. bacterial endotoxin, as well as by another type of carbohydrates, viz. ⁇ -1,3-glucans, which are part of the cell walls of essentially all fungi.
  • the 3-1,3-glucans very specifically activate a serine protease which, in addition to converting coagulogen into coagulin, converts prophenoloxidase into the active enzyme phenoloxidase.
  • a fungal or bacterial infection may thus rapidly and easily be detected by, in a per se known manner, contacting a sample to be examined with, on one hand, a blood cell lysate from crustaceans or insects, or an activable serine protease or proteases isolated therefrom, and, on the other hand, a detector substance which through the enzymatic action by such a blood cell lysate activated by a bacterial or fungal extract may form a physically or chemically detectable compound, and determining the latter.
  • a corresponding reagent or reagent kit for detecting or determining fungal or bacterial infections therefore comprises, on one hand, a blood cell lysate from crustaceans or insects and, on the other hand, such a detector substance.
  • Fresh-water decapods as well as marine decapods may be used.
  • fresh-water crayfish may be mentioned Astacus astacus (river crayfish), Pacifastacus leniusculus (signal crayfish), Astacus pallipes, Orconectes limosus, Astacus leptodactylus, Cambarus affinis (North-American crayfish), Procambarus ciarkii.
  • insects particularly those of Orthoptera and Lepidoptera
  • Schistocerca gregaria desert locust
  • Locusta migratoria common locust
  • Bombyx mori may be mentioned. Although insects probably would not be of the same interest for lysate production as crustaceans, the culture of, for example, silk-moth for this purpose might very well be contemplated. Due to the fact that blood cell lysates from, e.g., the above mentioned crustaceans may be used, a simple and continuous source of blood cell lysates having a very uniform quality is assured, since hemolymph from, e.g., crayfish may be collected during the major part of the year. The hemolymph of the horseshoe crab, on the other hand, may only be collected during a very limited period of time.
  • the invention comprises a method and a reagent, wherein the detector substance, i.e. the substance to be affected by the activated lysate, is a peptide compound of the formula
  • R 1 -X-Arg-R 2 wherein R 1 is a peptide moiety protected at the N-terminal and having at least two amino acid units, X is Gly or Ala, preferably Gly, and R 2 is a residue attached to the C-terminal of the arginine residue represented by Arg through an acide amide and/or ester linkage, and which in the presence of the blood cell lysate activated by bacteria or fungi may be hydrolyzed enzymatically into R 2 H, and/or a mineral acid salt thereof.
  • the residue R 2 is further such that the compound R 2 H formed may be detected physically or chemically, e.g.
  • the group R 2 is derived from p-nitroanilide, 5-nitro- ⁇ -naphtylamide, ⁇ -naphtylamide, ⁇ -naphtyl ester, ⁇ -naphtyl ester, indoxyl ester, N-methylindoxyl ester, (4-methyl)umbelliferyl ester and/or resorfin ester, the corresponding compounds R 2 H being p-nitroaniline, 5-nitro- ⁇ -naphtylamine, ⁇ -naphtylamine, ⁇ -naphtol, ⁇ -naphtol, indoxyl, N-methyl- indoxyl, 4-methyI-umbeliiferon and resorfin.
  • the first two compounds are chromogenic, while the other are fluorescent
  • Suitable protecting groups for R 1 are, for example, benzoyl, acetyl, carbobensoxy, tert-butoxycarbonyl and p-toluenesulf onyl.
  • -PNA p-nitroanilide
  • a hemocyte lysate i.e. a blood cell lysate, from crustaceans and insects according to the invention may be prepared essentially in the same way as the well known Limulus lysate from the horseshoe crab. This method is well described previously in the literature and need therefore not be described in any detail herein.
  • a partially purified hemocyte lysate from, for example, crustaceans is prepared by first collecting blood from the animal, care being taken to avoid contamination of the blood.
  • a crustacean which can be cultured in an aquaculture such as crayfish, signal crayfish, etc.
  • blood may be collected from the same animal several times at regular intervals as with a human blood donor.
  • the hemocytes or blood cells are then isolated through centrifuging and washing in conventional manner. After that they are homogenized in a buffer with a high calcium ion concentration, centrifuged at about 70,000 g and the supernatant recovered.
  • the lysate obtained is more stable than the present commercial lysates from horseshoe crabs and will remain stable for at least 24 hours.
  • the supernatant obtained is freeze-dried to be diluted with water or a suitable buffer (pH ⁇ 8) at the time of use.
  • the solution may optionally be stabilized with 0.5 - 1.5M NaCl, whereby a stability of several days may be achieved.
  • a solution of the freeze-dried lysate is stable for at least 5 hours.
  • bovine serum albumin and/or glycine may be added.
  • a reagent or reagent kit according to the invention for detecting fungal and bacterial infections may comprise a blood cell lysate prepared as above and a detector substance according to the previous definition.
  • the lysate and the detector substance are in powder form.
  • the test reagent is dissolved in a suitable buffer (pH ⁇ 8), and then the extract to be tested is added.
  • the reagent solution is then studied, for example, spectrophoto- metrically or colorimetrically depending on the detector substance used.
  • the method and the reagent of the invention are, in comparison with the horseshoe crab lysate known for endotoxin determination, also extremely sensitive for detecting fungal infections.
  • All fungi containing ⁇ -1,3-glucans in the cell walls thereof may be detected, which applies to all existing fungi with few exceptions.
  • To rapidly be able to detect fungal infections in accordance with the invention is of great value.
  • fungal skin infections on humans and animals are cultured, which takes about 2 weeks.
  • mould infections in food, so-called mycotoxins are becoming a rapidly increasing problem.
  • the sensitivities hitherto obtained with the use of lysates from crustaceans according to the invention are about 10 -8 - 10 -9 g/ml to endo toxins (bacterial infection) and about 10 -10 g/ml to ⁇ -1,3-glucans (fungal infection).
  • the sensitivity to endotoxins may probably be increased further by eliminating inhibitors of the endotoxin activation which have been shown to be included in the lysate, for example analogously to what is now done with the commercial horseshoe crab lysates.
  • the blood cell lysates may be rendered endotoxin specific by adding an excess of ⁇ -1,3-glucans.
  • ⁇ -1,3-glucan specificity may be achieved by adding anti-endotoxin factors, produced in pure form from crayfish lysate, which will then prevent the endotoxin activation of the crayfish lysate.
  • high contents of endotoxin (LPS) may be added.
  • Quantitative determinations of endotoxins and ⁇ -1,3-glucans, respectively, by means of the inventive process may be effected in a manner known per se, e.g. by providing a standard or calibration curve.
  • Example 1 Preparation of a hemocyte lysate Hemocytes from crayfish, Astacus astacus, were collected as described in S ⁇ derhall, K., Häll, L., Unestam, T., and Nyhlen, L. (1979) J. Invertebr. Pathol. 34, 285-294, except that 0.1M sodium citrate was excluded.
  • the hemocytes were homogenized in 10 mM sodium cacodylate buffer, pH 7.0, with 100 mM CaCl 2 and the homogenate was then centrifuged for 20 minutes at 70,000 g.
  • the supernatant obtained containing approximately 2 mg protein/ml, may be used either immediately or freeze-dried in 3 ml aliquots. Prior to use it is dissolved in 3 ml of distilled water to a final protein concentration of 2 mg/ml.
  • the ⁇ -1,3-glucans used were Zs (the supernatant of a 1% suspension of yeast cell walls, Zymosan, Sigma), Iaminaran M, laminaran G and a linear pentasaccharide composed of ⁇ -1,3-D-linked glucosyl residues.
  • Laminaran M and G were purified from laminaran (Sigma) by using DEAE-moIybdate-Sephadex ® chromatography according to Stark S., J.R. (1976) Carbohydr. Res. 47, 176-178.
  • the linear pentasaccharide was prepared and purified as described in S ⁇ derphinll, K., and Unestam, T. (1979) Can. J. Microbiol. 25, 406-414.
  • Example 4 A reagent according to the invention consisting of a crayfish hemocyte lysate according to Example 1 in 0.01 M cacodylate buffer (pH 7.0) and an equal amount (about 100 ⁇ l) of Bz-Ile-GIu( -piperidyl)-Gly-Arg-PNA.HCl were mixed with pre-heated (5 minutes, 100 ⁇ C) extracts of the following fungi: Aphanomyces astaci, Aphanomyces lae ⁇ is, Aphanomyces euteiches, Saecharomyces cerevisiae, Aspergillus flavus, Penicillium viridicatum, Candida albicans, Polyporus annosus, Boletus variegatus.
  • Example 5 A mixture of 100 ⁇ l of hemocyte lysate from Example 1, 100 ⁇ l of
  • E. coli endotoxin (Mallinckrodt, Inc., USA) of different concentrations, 100 ⁇ l of 0.1 M tris-HCl, pH 8.0, and 100 ⁇ l of a 2 mM solution of Bz-Ile-Glu( - piperidyl)-Gly-Arg-PNA.HCI (from Kabi Peptide Research Ltd., M ⁇ lndal, Sweden) were incubated for 30 minutes at 37°C. 100 ⁇ l of 50% acetic acid were then added to terminate the reaction, and the released p-nitroaniline was measured spectrophotometrically at 405 nm.
  • the absorbance changes obtained appear from Table 3:

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Abstract

Procédé de détection d'une infection fongueuse ou bactérienne en mettant en contact un échantillon à analyser avec (A) un lysat de cellules sanguines provenant d'un crustacé ou d'un insecte et (B) une substance détectrice sous la forme d'un composé peptide ayant un groupe terminal spécifique qui, par l'action enzymatique d'un lysat de cellules sanguines obtenu à partir d'un tel animal et activé par une bactérie ou un fongus peut être clivé pour former un composé physiquement ou chimiquement détectable. L'invention concerne également un agent de réaction ou un "kit" d'agents de réaction comprenant ce lysat de cellules sanguines et cette substance de détection.
PCT/SE1982/000430 1981-12-17 1982-12-17 PROCEDE ET AGENT DE REACTION POUR DETECTER DES ENDOTOXINES OU DES 'beta'-1,3 GLUCANES A PARTIR DE CHAMPIGNONS OU BACTERIES WO1983002123A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP83500092A JPS58502082A (ja) 1981-12-17 1982-12-17 細菌及び菌類の検出のための方法及び試薬

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
SE8107599-6811217 1981-12-17
SE8107599A SE431228B (sv) 1981-12-17 1981-12-17 Sett att bestemma bakteriella endotoxin medelst profenoloxidashaltigt blodkroppslysat fran kreftdjur eller insekter och reagens herfor

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WO1983002123A1 true WO1983002123A1 (fr) 1983-06-23

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EP (1) EP0096689A1 (fr)
JP (1) JPS58502082A (fr)
SE (1) SE431228B (fr)
WO (1) WO1983002123A1 (fr)

Cited By (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0270039A2 (fr) * 1986-12-03 1988-06-08 Wako Pure Chemical Industries Ltd Réactifs pour la détermination de peptidoglycane et bêta-1,3-glucane
EP0330991A2 (fr) * 1988-02-27 1989-09-06 Wako Pure Chemical Industries Ltd Procédé pour mesurer l'endotoxine
EP0333187A1 (fr) * 1988-03-16 1989-09-20 Wako Pure Chemical Industries Ltd Procédé de préparation d'un réactif pour la mesure d'endotoxines
WO1991006867A1 (fr) * 1989-11-01 1991-05-16 Atlantic Institute Of Biotechnology Agglutinine d'echinoderme et procede d'extraction associe
WO1991009052A1 (fr) * 1989-12-12 1991-06-27 Kabi Diagnostica Ab Substrat chromogene
EP0657546A1 (fr) * 1993-11-18 1995-06-14 Wako Pure Chemical Industries, Ltd. Procédé de dosage de l'activité d'enzyme activante de prophénoloxidase
US5594113A (en) * 1988-06-23 1997-01-14 Associates Of Cape Cod, Inc. Endotoxin binding and neutralizing protein and uses thereof
EP0757103A2 (fr) * 1995-07-31 1997-02-05 Wako Pure Chemical Industries Ltd Méthode pour la détection de microorganismes
US5681710A (en) * 1991-03-14 1997-10-28 Seikagaku Kogyo Kabushiki Kaisha Reagent for determining (1→3)-β-D-glucan
EP0924220A2 (fr) * 1997-12-16 1999-06-23 Wako Pure Chemical Industries, Ltd. Inhibiteur de l'activation d'une protéine reconnaissant de beta-glucane
WO2006076617A2 (fr) * 2005-01-13 2006-07-20 Charles River Laboratories, Inc. Procede de classification d'un micro-organisme dans un echantillon biologique
US7329538B2 (en) 2003-03-17 2008-02-12 Charles River Laboratories, Inc. Methods and compositions for the detection of microbial contaminants
US7598054B2 (en) 2003-10-31 2009-10-06 Immunetics, Inc. Rapid peptidoglycan-based assay for detection of bacterial contamination of platelets
US7968280B2 (en) 2004-12-02 2011-06-28 Charles River Laboratories, Inc. Methods for the detection and/or quantification of gram positive bacterial contaminants
US8450079B2 (en) 2003-10-31 2013-05-28 Immunetics, Inc. Method for detecting bacteria
WO2018236861A1 (fr) * 2017-06-19 2018-12-27 Inspirotec, Inc. (1-->3)-β-D-GLUCANE COMME MESURE DE MOISISSURES ACTIVES

Families Citing this family (1)

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Publication number Priority date Publication date Assignee Title
CN1206365C (zh) 2000-01-20 2005-06-15 株式会社三养吉尼克斯 用于检测β－1,3－葡聚糖的组合物,其制备方法和检测β－1,3－葡聚糖的诊断试剂盒

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DE2740323B2 (de) * 1977-06-14 1979-10-25 Seikagaku Kogyo Co., Ltd., Tokio Verfahren zur Bestimmung eines bakteriellen Endotoxins und Reagenz zur Verwendung bei diesem Verfahren
US4301245A (en) * 1980-05-29 1981-11-17 Dynasciences Corporation Chromogenic method of detecting endotoxins in blood
EP0056210A2 (fr) * 1981-01-09 1982-07-21 Centre National De La Recherche Scientifique (Cnrs) Procédé pour le dosage fluorimétrique des endotoxines, nouveaux peptides portant un fluorophore utilisables dans ledit procédé et leur méthode de préparation

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DE2740323B2 (de) * 1977-06-14 1979-10-25 Seikagaku Kogyo Co., Ltd., Tokio Verfahren zur Bestimmung eines bakteriellen Endotoxins und Reagenz zur Verwendung bei diesem Verfahren
US4301245A (en) * 1980-05-29 1981-11-17 Dynasciences Corporation Chromogenic method of detecting endotoxins in blood
EP0041089A2 (fr) * 1980-05-29 1981-12-09 Whittaker Bioproducts, Inc. Procédé chromogène pour la détection d'une endotoxine dans le sang
EP0056210A2 (fr) * 1981-01-09 1982-07-21 Centre National De La Recherche Scientifique (Cnrs) Procédé pour le dosage fluorimétrique des endotoxines, nouveaux peptides portant un fluorophore utilisables dans ledit procédé et leur méthode de préparation

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Chemical Abstracts Vol 94(1981), abstract No 151160u, Progr. Clin. Biol. Res. 1979, 29, 209-20. *
Chemical Abstracts Vol 94(1981), abstract No 2223q, FEBS Lett. 1980, 120(2), 217-20. *
Chemical Abstracts Vol 95(1981), abstract No 181776n, Clin. Chim. Acta 1981, 116(1), 63-8. *
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Cited By (35)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0270039A2 (fr) * 1986-12-03 1988-06-08 Wako Pure Chemical Industries Ltd Réactifs pour la détermination de peptidoglycane et bêta-1,3-glucane
EP0270039A3 (fr) * 1986-12-03 1991-06-05 Wako Pure Chemical Industries Ltd Réactifs pour la détermination de peptidoglycane et bêta-1,3-glucane
EP0330991A3 (fr) * 1988-02-27 1991-06-19 Wako Pure Chemical Industries Ltd Procédé pour mesurer l'endotoxine
EP0330991A2 (fr) * 1988-02-27 1989-09-06 Wako Pure Chemical Industries Ltd Procédé pour mesurer l'endotoxine
EP0333187A1 (fr) * 1988-03-16 1989-09-20 Wako Pure Chemical Industries Ltd Procédé de préparation d'un réactif pour la mesure d'endotoxines
US5594113A (en) * 1988-06-23 1997-01-14 Associates Of Cape Cod, Inc. Endotoxin binding and neutralizing protein and uses thereof
US5614369A (en) * 1988-06-23 1997-03-25 Associates Of Cape Cod, Inc. Endotoxin binding and neutralizing protein and uses thereof
US5627266A (en) * 1988-06-23 1997-05-06 Associates Of Cape Cod, Inc. Endotoxin binding and neutralizing protein and uses thereof
US5747455A (en) * 1988-06-23 1998-05-05 Associates Of Cape Cod, Inc. Endotoxin binding and neutralizing protein and uses thereof
US6384200B1 (en) 1988-06-23 2002-05-07 Associates Of Cape Cod, Inc. Endotoxin binding and neutralizing protein and uses thereof
WO1991006867A1 (fr) * 1989-11-01 1991-05-16 Atlantic Institute Of Biotechnology Agglutinine d'echinoderme et procede d'extraction associe
WO1991009052A1 (fr) * 1989-12-12 1991-06-27 Kabi Diagnostica Ab Substrat chromogene
US5681710A (en) * 1991-03-14 1997-10-28 Seikagaku Kogyo Kabushiki Kaisha Reagent for determining (1→3)-β-D-glucan
EP0657546A1 (fr) * 1993-11-18 1995-06-14 Wako Pure Chemical Industries, Ltd. Procédé de dosage de l'activité d'enzyme activante de prophénoloxidase
EP0757103A2 (fr) * 1995-07-31 1997-02-05 Wako Pure Chemical Industries Ltd Méthode pour la détection de microorganismes
EP0757103A3 (fr) * 1995-07-31 1997-12-29 Wako Pure Chemical Industries Ltd Méthode pour la détection de microorganismes
EP0924220A3 (fr) * 1997-12-16 2000-04-26 Wako Pure Chemical Industries, Ltd. Inhibiteur de l'activation d'une protéine reconnaissant de beta-glucane
US6274565B1 (en) 1997-12-16 2001-08-14 Wako Pure Chemical Industries, Ltd. Inhibitor of activation of β-glucan recognition protein
EP0924220A2 (fr) * 1997-12-16 1999-06-23 Wako Pure Chemical Industries, Ltd. Inhibiteur de l'activation d'une protéine reconnaissant de beta-glucane
US7939291B2 (en) 2003-03-17 2011-05-10 Charles River Laboratories, Inc. Methods for the detection of microbial contaminants
US10119969B2 (en) 2003-03-17 2018-11-06 Charles River Laboratories, Inc. Compositions for the detection of microbial contaminants
US7329538B2 (en) 2003-03-17 2008-02-12 Charles River Laboratories, Inc. Methods and compositions for the detection of microbial contaminants
US8841086B2 (en) 2003-10-31 2014-09-23 Immunetics, Inc. Kit for detecting bacterial contamination
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SE431228B (sv) 1984-01-23
SE8107599L (sv) 1983-06-18
EP0096689A1 (fr) 1983-12-28
JPS58502082A (ja) 1983-12-08

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