CA1107646A - Anti-microbial composition - Google Patents

Anti-microbial composition

Info

Publication number: CA1107646A
Authority: CA; Canada
Prior art keywords: glucanase; physarum; beta; extract; alpha
Prior art date: 1977-03-28
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired

Application number

CA299,788A

Other languages

English (en)

French (fr)

Inventor

David A.L. Davies

Anthony M.S. Pope

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

GD Searle LLC

Original Assignee

GD Searle LLC

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1977-03-28

Filing date

1978-03-28

Publication date

1981-08-25

1978-03-28 Application filed by GD Searle LLC filed Critical GD Searle LLC

1981-08-25 Application granted granted Critical

1981-08-25 Publication of CA1107646A publication Critical patent/CA1107646A/en

Status Expired legal-status Critical Current

Links

239000000203 mixture Substances 0.000 title abstract description 16
230000000845 anti-microbial effect Effects 0.000 title abstract description 5
239000004599 antimicrobial Substances 0.000 title abstract description 3
239000000284 extract Substances 0.000 claims abstract description 56
241000224485 Physarum Species 0.000 claims abstract description 49
102000004190 Enzymes Human genes 0.000 claims abstract description 36
108090000790 Enzymes Proteins 0.000 claims abstract description 36
229940088598 enzyme Drugs 0.000 claims description 32
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 20
238000000034 method Methods 0.000 claims description 17
230000000694 effects Effects 0.000 claims description 16
102000012286 Chitinases Human genes 0.000 claims description 9
108010022172 Chitinases Proteins 0.000 claims description 9
108010014251 Muramidase Proteins 0.000 claims description 9
102000016943 Muramidase Human genes 0.000 claims description 9
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 9
239000007788 liquid Substances 0.000 claims description 9
108010055851 Acetylglucosaminidase Proteins 0.000 claims description 6
239000006228 supernatant Substances 0.000 claims description 5
241000224486 Physarum polycephalum Species 0.000 claims description 4
238000004519 manufacturing process Methods 0.000 claims description 4
239000000047 product Substances 0.000 claims description 4
102100036495 Di-N-acetylchitobiase Human genes 0.000 claims description 3
239000002510 pyrogen Substances 0.000 claims description 3
101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 claims description 2
238000005119 centrifugation Methods 0.000 claims description 2
238000001556 precipitation Methods 0.000 claims description 2
229940126601 medicinal product Drugs 0.000 claims 6
239000001963 growth medium Substances 0.000 claims 2
239000012535 impurity Substances 0.000 claims 1
238000009630 liquid culture Methods 0.000 claims 1
239000002904 solvent Substances 0.000 claims 1
239000003429 antifungal agent Substances 0.000 abstract description 8
230000002101 lytic effect Effects 0.000 abstract description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 23
239000011780 sodium chloride Substances 0.000 description 23
APKFDSVGJQXUKY-INPOYWNPSA-N amphotericin B Chemical compound O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1/C=C/C=C/C=C/C=C/C=C/C=C/C=C/[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 APKFDSVGJQXUKY-INPOYWNPSA-N 0.000 description 16
APKFDSVGJQXUKY-KKGHZKTASA-N Amphotericin-B Natural products O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1C=CC=CC=CC=CC=CC=CC=C[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 APKFDSVGJQXUKY-KKGHZKTASA-N 0.000 description 15
229960003942 amphotericin b Drugs 0.000 description 15
208000015181 infectious disease Diseases 0.000 description 11
241001465754 Metazoa Species 0.000 description 9
210000004027 cell Anatomy 0.000 description 9
241000222511 Coprinus Species 0.000 description 8
235000010335 lysozyme Nutrition 0.000 description 8
241000699670 Mus sp. Species 0.000 description 7
230000001857 anti-mycotic effect Effects 0.000 description 6
230000002538 fungal effect Effects 0.000 description 6
229940051921 muramidase Drugs 0.000 description 6
229960000988 nystatin Drugs 0.000 description 6
VQOXZBDYSJBXMA-NQTDYLQESA-N nystatin A1 Chemical compound O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1/C=C/C=C/C=C/C=C/CC/C=C/C=C/[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 VQOXZBDYSJBXMA-NQTDYLQESA-N 0.000 description 6
238000011282 treatment Methods 0.000 description 6
239000002543 antimycotic Substances 0.000 description 5
239000000725 suspension Substances 0.000 description 5
241000222065 Lycoperdon Species 0.000 description 4
239000008194 pharmaceutical composition Substances 0.000 description 4
238000002560 therapeutic procedure Methods 0.000 description 4
CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
241001225321 Aspergillus fumigatus Species 0.000 description 3
241000222122 Candida albicans Species 0.000 description 3
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
208000031888 Mycoses Diseases 0.000 description 3
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
230000001580 bacterial effect Effects 0.000 description 3
210000002421 cell wall Anatomy 0.000 description 3
KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
239000000287 crude extract Substances 0.000 description 3
239000003814 drug Substances 0.000 description 3
229940079593 drug Drugs 0.000 description 3
238000009472 formulation Methods 0.000 description 3
238000000338 in vitro Methods 0.000 description 3
239000007928 intraperitoneal injection Substances 0.000 description 3
238000001990 intravenous administration Methods 0.000 description 3
230000009467 reduction Effects 0.000 description 3
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
201000002909 Aspergillosis Diseases 0.000 description 2
241000228212 Aspergillus Species 0.000 description 2
208000036641 Aspergillus infections Diseases 0.000 description 2
241000700198 Cavia Species 0.000 description 2
241000191938 Micrococcus luteus Species 0.000 description 2
241001045770 Trichophyton mentagrophytes Species 0.000 description 2
230000000844 anti-bacterial effect Effects 0.000 description 2
229940091771 aspergillus fumigatus Drugs 0.000 description 2
238000011888 autopsy Methods 0.000 description 2
229940095731 candida albicans Drugs 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
230000034994 death Effects 0.000 description 2
231100000517 death Toxicity 0.000 description 2
230000000593 degrading effect Effects 0.000 description 2
239000012153 distilled water Substances 0.000 description 2
239000003937 drug carrier Substances 0.000 description 2
239000008103 glucose Substances 0.000 description 2
229960000274 lysozyme Drugs 0.000 description 2
239000004325 lysozyme Substances 0.000 description 2
230000003287 optical effect Effects 0.000 description 2
239000000243 solution Substances 0.000 description 2
230000004083 survival effect Effects 0.000 description 2
230000002195 synergetic effect Effects 0.000 description 2
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
229930183010 Amphotericin Natural products 0.000 description 1
QGGFZZLFKABGNL-UHFFFAOYSA-N Amphotericin A Natural products OC1C(N)C(O)C(C)OC1OC1C=CC=CC=CC=CCCC=CC=CC(C)C(O)C(C)C(C)OC(=O)CC(O)CC(O)CCC(O)C(O)CC(O)CC(O)(CC(O)C2C(O)=O)OC2C1 QGGFZZLFKABGNL-UHFFFAOYSA-N 0.000 description 1
238000011725 BALB/c mouse Methods 0.000 description 1
241000894006 Bacteria Species 0.000 description 1
108010023063 Bacto-peptone Proteins 0.000 description 1
101100290380 Caenorhabditis elegans cel-1 gene Proteins 0.000 description 1
241000222120 Candida <Saccharomycetales> Species 0.000 description 1
206010007134 Candida infections Diseases 0.000 description 1
208000007163 Dermatomycoses Diseases 0.000 description 1
ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 description 1
206010017533 Fungal infection Diseases 0.000 description 1
241000233866 Fungi Species 0.000 description 1
241000282560 Macaca mulatta Species 0.000 description 1
GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
241000282344 Mellivora capensis Species 0.000 description 1
240000007594 Oryza sativa Species 0.000 description 1
235000007164 Oryza sativa Nutrition 0.000 description 1
240000004808 Saccharomyces cerevisiae Species 0.000 description 1
229920002125 Sokalan® Polymers 0.000 description 1
229920002472 Starch Polymers 0.000 description 1
JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
206010067409 Trichophytosis Diseases 0.000 description 1
230000005856 abnormality Effects 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
229910052921 ammonium sulfate Inorganic materials 0.000 description 1
235000011130 ammonium sulphate Nutrition 0.000 description 1
229940009444 amphotericin Drugs 0.000 description 1
229960002685 biotin Drugs 0.000 description 1
235000020958 biotin Nutrition 0.000 description 1
239000011616 biotin Substances 0.000 description 1
230000037396 body weight Effects 0.000 description 1
201000003984 candidiasis Diseases 0.000 description 1
150000001720 carbohydrates Chemical class 0.000 description 1
235000014633 carbohydrates Nutrition 0.000 description 1
238000002512 chemotherapy Methods 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
239000012228 culture supernatant Substances 0.000 description 1
238000005520 cutting process Methods 0.000 description 1
201000003929 dermatomycosis Diseases 0.000 description 1
239000008121 dextrose Substances 0.000 description 1
239000002552 dosage form Substances 0.000 description 1
238000000605 extraction Methods 0.000 description 1
XRECTZIEBJDKEO-UHFFFAOYSA-N flucytosine Chemical compound NC1=NC(=O)NC=C1F XRECTZIEBJDKEO-UHFFFAOYSA-N 0.000 description 1
229960004413 flucytosine Drugs 0.000 description 1
244000053095 fungal pathogen Species 0.000 description 1
230000000855 fungicidal effect Effects 0.000 description 1
239000000417 fungicide Substances 0.000 description 1
229930182830 galactose Natural products 0.000 description 1
238000001641 gel filtration chromatography Methods 0.000 description 1
150000004676 glycans Chemical class 0.000 description 1
BTIJJDXEELBZFS-UHFFFAOYSA-K hemin Chemical compound [Cl-].[Fe+3].[N-]1C(C=C2C(=C(C)C(C=C3C(=C(C)C(=C4)[N-]3)C=C)=N2)C=C)=C(C)C(CCC(O)=O)=C1C=C1C(CCC(O)=O)=C(C)C4=N1 BTIJJDXEELBZFS-UHFFFAOYSA-K 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
238000011081 inoculation Methods 0.000 description 1
238000007912 intraperitoneal administration Methods 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
231100000053 low toxicity Toxicity 0.000 description 1
210000004072 lung Anatomy 0.000 description 1
239000000463 material Substances 0.000 description 1
238000005259 measurement Methods 0.000 description 1
238000005374 membrane filtration Methods 0.000 description 1
238000006213 oxygenation reaction Methods 0.000 description 1
244000052769 pathogen Species 0.000 description 1
230000001717 pathogenic effect Effects 0.000 description 1
239000000902 placebo Substances 0.000 description 1
229940068196 placebo Drugs 0.000 description 1
229920001282 polysaccharide Polymers 0.000 description 1
239000005017 polysaccharide Substances 0.000 description 1
229920000136 polysorbate Polymers 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
102000004169 proteins and genes Human genes 0.000 description 1
108090000623 proteins and genes Proteins 0.000 description 1
239000012521 purified sample Substances 0.000 description 1
210000005084 renal tissue Anatomy 0.000 description 1
230000029058 respiratory gaseous exchange Effects 0.000 description 1
230000004044 response Effects 0.000 description 1
235000009566 rice Nutrition 0.000 description 1
239000007787 solid Substances 0.000 description 1
241000894007 species Species 0.000 description 1
238000001228 spectrum Methods 0.000 description 1
235000019698 starch Nutrition 0.000 description 1
239000008107 starch Substances 0.000 description 1
239000000126 substance Substances 0.000 description 1
238000011287 therapeutic dose Methods 0.000 description 1
235000019157 thiamine Nutrition 0.000 description 1
KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
229960003495 thiamine Drugs 0.000 description 1
239000011721 thiamine Substances 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
230000000699 topical effect Effects 0.000 description 1
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
231100000820 toxicity test Toxicity 0.000 description 1
210000003462 vein Anatomy 0.000 description 1
238000005303 weighing Methods 0.000 description 1
210000005253 yeast cell Anatomy 0.000 description 1
229910000368 zinc sulfate Inorganic materials 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01108—Lactase (3.2.1.108)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/10—Antimycotics
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01021—Beta-glucosidase (3.2.1.21)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01025—Beta-mannosidase (3.2.1.25), i.e. mannanase
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01039—Glucan endo-1,3-beta-D-glucosidase (3.2.1.39)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01052—Beta-N-acetylhexosaminidase (3.2.1.52)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01058—Glucan 1,3-beta-glucosidase (3.2.1.58)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01073—Licheninase (3.2.1.73)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01075—Glucan endo-1,6-beta-glucosidase (3.2.1.75)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01078—Mannan endo-1,4-beta-mannosidase (3.2.1.78), i.e. endo-beta-mannanase
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01084—Glucan 1,3-alpha-glucosidase (3.2.1.84), i.e. mutanase
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
General Health & Medical Sciences (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Genetics & Genomics (AREA)
Bioinformatics & Cheminformatics (AREA)
Engineering & Computer Science (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Medicinal Chemistry (AREA)
Communicable Diseases (AREA)
Veterinary Medicine (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Public Health (AREA)
General Chemical & Material Sciences (AREA)
Pharmacology & Pharmacy (AREA)
Chemical Kinetics & Catalysis (AREA)
Oncology (AREA)
Animal Behavior & Ethology (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Enzymes And Modification Thereof (AREA)
Medicines Containing Plant Substances (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Medicinal Preparation (AREA)

CA299,788A 1977-03-28 1978-03-28 Anti-microbial composition Expired CA1107646A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
GB12919/77A GB1576891A (en)	1977-03-28	1977-03-28	Antimicrobial compositions containing extracts of light enzymes from physarum species
GB12919/77		1977-03-28

Publications (1)

Publication Number	Publication Date
CA1107646A true CA1107646A (en)	1981-08-25

Family

ID=10013545

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA299,788A Expired CA1107646A (en)	1977-03-28	1978-03-28	Anti-microbial composition

Country Status (20)

Country	Link
JP (1)	JPS542310A (de)
AT (1)	AT363589B (de)
AU (1)	AU519066B2 (de)
BE (1)	BE865369A (de)
CA (1)	CA1107646A (de)
DE (1)	DE2813282A1 (de)
DK (1)	DK134678A (de)
ES (1)	ES468236A1 (de)
FI (1)	FI780933A7 (de)
FR (1)	FR2385730A1 (de)
GB (1)	GB1576891A (de)
GR (1)	GR71706B (de)
IE (1)	IE46698B1 (de)
IL (1)	IL54364A0 (de)
NL (1)	NL7803291A (de)
NO (1)	NO781035L (de)
NZ (1)	NZ186783A (de)
PT (1)	PT67826B (de)
SE (1)	SE7803456L (de)
ZA (1)	ZA781758B (de)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
FR2569107A1 (fr) *	1984-08-17	1986-02-21	Squibb & Sons Inc	Suppositoires antifongiques adhesifs a longue duree

Families Citing this family (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS58134014A (ja) *	1982-02-03	1983-08-10	Rooto Seiyaku Kk	義歯洗浄用組成物
JPH0261164A (ja) *	1988-08-27	1990-03-01	Hisaka Works Ltd	処理槽への内槽装填・取り出し方法およびそれに用いる移載車。
JPH0261163A (ja) *	1988-08-27	1990-03-01	Hisaka Works Ltd	繊維材料取り出し方法およびそれに用いる装置
ES2172795T3 (es) *	1996-06-07	2002-10-01	Dsm Nv	Nuevos fungicidas enzimaticos.

1977
- 1977-03-28 GB GB12919/77A patent/GB1576891A/en not_active Expired
1978
- 1978-03-22 NO NO781035A patent/NO781035L/no unknown
- 1978-03-23 AU AU34479/78A patent/AU519066B2/en not_active Expired
- 1978-03-23 NZ NZ186783A patent/NZ186783A/xx unknown
- 1978-03-27 GR GR55801A patent/GR71706B/el unknown
- 1978-03-27 ES ES468236A patent/ES468236A1/es not_active Expired
- 1978-03-27 PT PT67826A patent/PT67826B/pt unknown
- 1978-03-27 JP JP3526978A patent/JPS542310A/ja active Pending
- 1978-03-27 IL IL54364A patent/IL54364A0/xx unknown
- 1978-03-28 DE DE19782813282 patent/DE2813282A1/de not_active Withdrawn
- 1978-03-28 SE SE7803456A patent/SE7803456L/xx unknown
- 1978-03-28 ZA ZA00781758A patent/ZA781758B/xx unknown
- 1978-03-28 AT AT0215978A patent/AT363589B/de not_active IP Right Cessation
- 1978-03-28 BE BE186314A patent/BE865369A/xx unknown
- 1978-03-28 DK DK134678A patent/DK134678A/da not_active Application Discontinuation
- 1978-03-28 NL NL7803291A patent/NL7803291A/xx not_active Application Discontinuation
- 1978-03-28 FR FR7808962A patent/FR2385730A1/fr active Granted
- 1978-03-28 FI FI780933A patent/FI780933A7/fi not_active Application Discontinuation
- 1978-03-28 CA CA299,788A patent/CA1107646A/en not_active Expired
- 1978-03-29 IE IE623/78A patent/IE46698B1/en unknown

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
FR2569107A1 (fr) *	1984-08-17	1986-02-21	Squibb & Sons Inc	Suppositoires antifongiques adhesifs a longue duree

Also Published As

Publication number	Publication date
FR2385730B1 (de)	1981-07-10
PT67826A (en)	1978-04-01
IE780623L (en)	1978-09-28
SE7803456L (sv)	1978-09-29
BE865369A (fr)	1978-09-28
ATA215978A (de)	1981-01-15
DE2813282A1 (de)	1978-10-12
ZA781758B (en)	1979-05-30
NO781035L (no)	1978-09-29
PT67826B (en)	1979-09-27
AU3447978A (en)	1979-09-27
DK134678A (da)	1978-09-29
IE46698B1 (en)	1983-08-24
FR2385730A1 (fr)	1978-10-27
NL7803291A (nl)	1978-10-02
JPS542310A (en)	1979-01-09
GR71706B (de)	1983-06-21
AU519066B2 (en)	1981-11-05
NZ186783A (en)	1980-12-19
GB1576891A (en)	1980-10-15
ES468236A1 (es)	1978-12-01
FI780933A7 (fi)	1978-09-29
IL54364A0 (en)	1978-06-15
AT363589B (de)	1981-08-10

Legal Events

Date	Code	Title	Description
1998-08-25	MKEX	Expiry
2023-05-26	MKEX	Expiry	Effective date: 19980825

Publication	Publication Date	Title
US4062941A (en)	1977-12-13	Method for treating fungal infections using cell lytic enzymes
Dubos et al.	1939	Studies on a bactericidal agent extracted from a soil bacillus: III. Preparation and activity of a protein-free fraction
KR101736790B1 (ko)	2017-05-17	바실러스, 히알루론산 효소, 및 그의 용도
Cunningham et al.	1951	508. Cordycepin, a metabolic product from cultures of Cordyceps militaris (Linn.) link. Part I. Isolation and characterisation
Trahan et al.	1985	Transport and phosphorylation of xylitol by a fructose phosphotransferase system in Streptococcus mutans
Shlaes et al.	1984	Infection caused by vancomycin-resistant Streptococcus sanguis II
CA1107646A (en)	1981-08-25	Anti-microbial composition
EP0201332B1 (de)	1992-09-02	Gegen Infektionen aktive Verbindung
Toews et al.	1985	Role of C5 and recruited neutrophils in early clearance of nontypable Haemophilus influenzae from murine lungs
US4144327A (en)	1979-03-13	Antimicrobial composition comprising lytic enzymes from physarum and an antimycotic agent
EP0964685B1 (de)	2005-06-08	Verfahren und zusammensetzung zur behandlung von mykosen in tieren
Cinco et al.	1983	A microbiological survey on the activity of a hydroalcoholic extract of camomile
Kligman et al.	1953	In vitro and in vivo activity of candicidin on pathogenic fungi
US5010062A (en)	1991-04-23	Therapeutic agent and method of inhibiting vascularization of tumors
Goitein et al.	1975	Penetration of parenterally administered gentamicin into the cerebrospinal fluid in experimental meningitis
WO1999058650A1 (en)	1999-11-18	Lytic enzymes useful for treating fungal infections
US3987164A (en)	1976-10-19	Method for prevention of pseudomonas aeruginosa infections
Callow et al.	1947	Licheniformin, an antibiotic substance from Bacillus licheniformis, active against Mycobacterium tuberculosis
RU2233171C2 (ru)	2004-07-27	ПОЛИФУНКЦИОНАЛЬНАЯ ФАРМАЦЕВТИЧЕСКАЯ КОМПОЗИЦИЯ НА ОСНОВЕ L-ЛИЗИН-α-ОКСИДАЗЫ ИЗ ГРИБА РОДА TRICHODERMA И СПОСОБ ПОЛУЧЕНИЯ ЭТОГО ФЕРМЕНТА
KANAOKA et al.	1987	Antitumor activity of streptococcal acid glycoprotein produced by Streptococcus pyogenes Su
Emmart et al.	1949	The tuberculostatic action of Nocardia extracts in white mice
KR920005685B1 (ko)	1992-07-13	유산균을 이용한 항 종양제
Eastridge JR et al.	1968	L-form infection of the rat kidney: effect of water diuresis
Jensen et al.	1964	Influence of endotoxin on the dermal response of rabbits to human oral bacteria
EP0661293A2 (de)	1995-07-05	Protein mit Zellwachstumsstimulierender und Makrophage chemotaktischer Wirkung, Verfahren zur Herstellung und Verwendung

CA1107646A - Anti-microbial composition - Google Patents

Info

Links

Classifications

Landscapes

Applications Claiming Priority (2)

Publications (1)

Family

ID=10013545

Family Applications (1)

Country Status (20)

Cited By (1)

Families Citing this family (4)

Cited By (1)

Also Published As

Similar Documents

Legal Events