EP0005131B1 - Methods and materials for cleaning soft contact lenses - Google Patents
Methods and materials for cleaning soft contact lenses Download PDFInfo
- Publication number
- EP0005131B1 EP0005131B1 EP79850032A EP79850032A EP0005131B1 EP 0005131 B1 EP0005131 B1 EP 0005131B1 EP 79850032 A EP79850032 A EP 79850032A EP 79850032 A EP79850032 A EP 79850032A EP 0005131 B1 EP0005131 B1 EP 0005131B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- lens
- enzyme
- lipase
- solution
- cleaning
- Prior art date
- 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
Links
- 238000004140 cleaning Methods 0.000 title claims description 37
- 238000000034 method Methods 0.000 title claims description 21
- 239000000463 material Substances 0.000 title description 11
- 239000000243 solution Substances 0.000 claims description 32
- 150000002632 lipids Chemical class 0.000 claims description 28
- 102000004190 Enzymes Human genes 0.000 claims description 27
- 108090000790 Enzymes Proteins 0.000 claims description 27
- 229940088598 enzyme Drugs 0.000 claims description 27
- 239000004365 Protease Substances 0.000 claims description 21
- 239000007788 liquid Substances 0.000 claims description 15
- 239000004367 Lipase Substances 0.000 claims description 14
- 108091005804 Peptidases Proteins 0.000 claims description 14
- 230000002366 lipolytic effect Effects 0.000 claims description 14
- 102000004882 Lipase Human genes 0.000 claims description 13
- 108090001060 Lipase Proteins 0.000 claims description 13
- 102000035195 Peptidases Human genes 0.000 claims description 13
- 235000019421 lipase Nutrition 0.000 claims description 13
- 102000004169 proteins and genes Human genes 0.000 claims description 13
- 108090000623 proteins and genes Proteins 0.000 claims description 13
- 108010004032 Bromelains Proteins 0.000 claims description 11
- 235000019835 bromelain Nutrition 0.000 claims description 11
- 229920000642 polymer Polymers 0.000 claims description 11
- 108010088751 Albumins Proteins 0.000 claims description 10
- 102000009027 Albumins Human genes 0.000 claims description 10
- 108090000526 Papain Proteins 0.000 claims description 9
- 229940055729 papain Drugs 0.000 claims description 9
- 235000019834 papain Nutrition 0.000 claims description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 9
- 230000002255 enzymatic effect Effects 0.000 claims description 8
- 239000008363 phosphate buffer Substances 0.000 claims description 8
- 239000002504 physiological saline solution Substances 0.000 claims description 6
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 claims description 4
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 claims description 4
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 claims description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 4
- 229930195725 Mannitol Natural products 0.000 claims description 4
- 238000009835 boiling Methods 0.000 claims description 4
- 239000000594 mannitol Substances 0.000 claims description 4
- 235000010355 mannitol Nutrition 0.000 claims description 4
- 239000000600 sorbitol Substances 0.000 claims description 4
- 235000010356 sorbitol Nutrition 0.000 claims description 4
- 239000001888 Peptone Substances 0.000 claims description 3
- 108010080698 Peptones Proteins 0.000 claims description 3
- 235000014113 dietary fatty acids Nutrition 0.000 claims description 3
- AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical class CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 claims description 3
- 150000002148 esters Chemical class 0.000 claims description 3
- 239000000194 fatty acid Substances 0.000 claims description 3
- 229930195729 fatty acid Natural products 0.000 claims description 3
- 150000004665 fatty acids Chemical class 0.000 claims description 3
- 235000019319 peptone Nutrition 0.000 claims description 3
- 229940066779 peptones Drugs 0.000 claims description 3
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 claims description 3
- 235000010262 sodium metabisulphite Nutrition 0.000 claims description 3
- 239000004296 sodium metabisulphite Substances 0.000 claims description 3
- 239000000126 substance Substances 0.000 claims description 3
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims description 3
- 239000000203 mixture Substances 0.000 claims 2
- 239000012530 fluid Substances 0.000 description 13
- 235000018102 proteins Nutrition 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 230000000694 effects Effects 0.000 description 8
- 238000002360 preparation method Methods 0.000 description 5
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical class C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 4
- 108010044091 Globulins Proteins 0.000 description 3
- 102000006395 Globulins Human genes 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000016943 Muramidase Human genes 0.000 description 3
- 108010014251 Muramidase Proteins 0.000 description 3
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 3
- 238000011835 investigation Methods 0.000 description 3
- 239000004325 lysozyme Substances 0.000 description 3
- 229960000274 lysozyme Drugs 0.000 description 3
- 235000010335 lysozyme Nutrition 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 2
- 102000004895 Lipoproteins Human genes 0.000 description 2
- 208000002193 Pain Diseases 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 235000012000 cholesterol Nutrition 0.000 description 2
- 239000012459 cleaning agent Substances 0.000 description 2
- 239000000644 isotonic solution Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 150000003904 phospholipids Chemical class 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- WOBHKFSMXKNTIM-UHFFFAOYSA-N Hydroxyethyl methacrylate Chemical compound CC(=C)C(=O)OCCO WOBHKFSMXKNTIM-UHFFFAOYSA-N 0.000 description 1
- -1 Ig y-globulin Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 241000519995 Stachys sylvatica Species 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000008135 aqueous vehicle Substances 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- HPNSNYBUADCFDR-UHFFFAOYSA-N chromafenozide Chemical compound CC1=CC(C)=CC(C(=O)N(NC(=O)C=2C(=C3CCCOC3=CC=2)C)C(C)(C)C)=C1 HPNSNYBUADCFDR-UHFFFAOYSA-N 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 239000000882 contact lens solution Substances 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- 238000002845 discoloration Methods 0.000 description 1
- RMGVZKRVHHSUIM-UHFFFAOYSA-L dithionate(2-) Chemical compound [O-]S(=O)(=O)S([O-])(=O)=O RMGVZKRVHHSUIM-UHFFFAOYSA-L 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000016507 interphase Effects 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 230000013190 lipid storage Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000000414 obstructive effect Effects 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920003229 poly(methyl methacrylate) Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 239000004926 polymethyl methacrylate Substances 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920001296 polysiloxane Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 239000004576 sand Substances 0.000 description 1
- 230000035807 sensation Effects 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000008247 solid mixture Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/0005—Other compounding ingredients characterised by their effect
- C11D3/0078—Compositions for cleaning contact lenses, spectacles or lenses
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
Definitions
- the present invention relates to a method and materials for removing from soft contact lenses deposits that are formed during use.
- Such deposits contain mainly albumin, globulins and lipids.
- Deposits that occur during use of soft contact lenses generally result in an opaque film, yellow discoloration, white spots and thread-like configurations on the lenses. Investigations carried out have shown that these deposits can consist of albumin, Ig y-globulin, Lysozyme and lipoproteins.
- the deposits are often largely composed of lipids and denatured albumin, which are deposited on the lenses from the tear fluid as a result of the saline solution with which the lenses are impregnated being exchanged for the tear fluid.
- the drying-out of a lens for instance through its use in a dry environment and by air flowing past it, etc. causes some albumin to be denatured and deposited on the lens.
- albumin is denatured which gives rise to apolar interior groups of lipids.
- Other causes too such as for example continuous use, cause albumin and lipids to be deposited on contact lenses in fairly large quantities.
- One method of cleaning contact lenses is already known which comprises the steps of dissolving in water a proteolytic enzyme in tablet form and then placing the lenses to be cleaned in the solution for a period of at least two hours.
- This process has been regarded as complicated by the wearers of contact lenses so that cleaning has not always been carried out as regularly as is required and this has resulted in lenses finally acquiring such a coating that the lenses have become unusable.
- the prior art using only proteolytic enzymes does not provide for complete removal of the deposits formed in that deposits of lipid origin remain substantially unaffected by the solutions of the prior art.
- An object of the present invention is to provide cleaning solutions and methods for cleaning soft contact lenses which, on the one hand are simple for the contact lens wearer to use and which also provide an improved cleaning effect.
- Yet another object of the present invention is to provide solid compositions of matter to be dissolved in an aqueous vehicle to form soft contact lens cleaning solutions, preferably of a hypertonic character.
- an enzyme containing cleaning liquid for soft contact lenses consists of a solution containing a lipolytic enzyme (mainly for reducing the lipids) and a proteolytic enzyme, such as papain or bromelain, (for reducing the albumin deposits) and, additionally, a phosphate buffering agent.
- a lipolytic enzyme mainly for reducing the lipids
- a proteolytic enzyme such as papain or bromelain
- a phosphate buffering agent preferably hypertonic to its nature, i.e. its osmotic pressure exceeds that of a physiological solution, so that in treatment with the solution some dewatering of the lens takes place, which seems to be beneficial to the cleaning effect.
- an isotonic solution for example a saline solution
- the lens reversibly again takes up water to revert to its original state.
- a pack for cleaning soft contact lenses comprises a volume of a solution containing papain or bromelain and a lipolytic enzyme, a device for forming droplets of the solution for depositing same on the surface of a soft contact lens and a volume of a sterile isotonic physiological saline solution in which the lens can be rinsed and subsequently boiled.
- the method of cleaning a soft contact lens in accordance with the invention to remove deposits on the surface of the lens by enzymatic action comprises the steps of placing at least one drop of a solution containing a proteolytic enzyme, such as papain or bromelain, and in addition a lipolytic enzyme, on the contact lens which is to be cleaned to reduce both albumin and lipids present to water soluble peptones, fatty acids and esters, and subsequently removing the resulting products by rinsing and boiling the lens in a physiological saline solution.
- a proteolytic enzyme such as papain or bromelain
- the enzyme activity in the cleaning solution is of the order of 100 tyrosine units per ,ug of protein.
- the fluid activity is allowed to occur for a period of the order of 15 minutes.
- the physiological saline solution has a particle size below 0.2 microns, and is isotonic, has a pH-value of 7.0 with a buffer capacity of 6-8 and is also sterile.
- a preferred enzyme solution for cleaning the lens consists of bromelain, mannitol, sorbitol, ethylenediamine tetraacetic acid, sodium metabisulphite, and a lipolytic enzyme.
- a preferred cleaning solution may consist of: diluted to 1 litre aqua dest., together with lipase from cand. cylindracae, preferably in an amount corresponding to 50000 units, in 1000 ml. 0.1 M phosphate buffer in an aqueous polymer complex.
- aqueous polymer complex which is conventional in the art and have for a purpose to bind the lipolytic enzymes so that it will not be unduly destroyed by the proteolytic enzyme.
- the nature of this polymer complex is not critical and any commercial product may be used, such as polyethylene glycol, polyvinyl alcohol, polyvinyl pyrrolidone and the like. As a fully non-limiting example one may mention the polymer complex "Kollodon" 25 or 30 from BASF, West Germany.
- PMMA, HEMA and PvP all have a common factor, that is, they are lipid and protein retensive. New materials have been introduced such as silicone, even in this material there is lipid retention.
- the lipid deposits appear either as yellowish tinting of the lens or as a whitish haze.
- the deposits are composed of phospholipids, probably in the form of lecitin, forming together with the protein a lecitoprotein, (lecitin on exposure to heat and light tends to autooxidise or decompose into yellowish substances) or cholesterol and fat esters which are white in colour.
- plaque consists of a central core of lipid lying free on the polymer and protruding into the material matric causing a sand grain sensation when the lens lies in the eye.
- any lipolytic enzyme hydrolyzing the lipids to yield fatty acids and glycerol are useful.
- a preferred variety is lipase derived from cand. cylindracae, suitably prepared by lyophilization.
- a proteolytic enzyme any protein- digesting enzyme is useful, preferred examples being bromelain and papain.
- a lipolytic enzyme and a proteolytic enzyme the latter being papain, it will be noted that the beneficial effect of free sulfhydryl groups on the activity of papain will be satisfied by the presence of the lipase containing sulfhydryl groups.
- such combination of enzymes is particularly preferred, especially when used in solutions of a hypertonic character.
- a soft contact lens cleaning fluid (known as Prolen) is made up as follows: Then add:-Lipase from cand. cylindracae 50000 units in 1000 ml 0.1 M Phosphate buffer in an aqueous polymer complex.
- a few drops (0.3 ml) of the fluid are placed on a lens and left on the lens for 15 minutes.
- the lens is then rinsed in a saline solution and thereafter boiled in the saline solution for 20 minutes. Finally the lens is rinsed once more in the saline solution before reinserting.
- a lens is usually coated with deposits of protein, lipoproteins and lipids.
- the lens is treated with a preparation having a high enzymatic effect which contains a stabilised protease and a high activity lipase. Drops of the preparation are placed on the lens in accordance with the invention and it is left for the preparation to take effect, for 15 minutes.
- This cleaning preparation is, as described above, preferably formed from Bromelain, Mannitol, Sorbitol, Ethylenediaminetetraacetic acid, Sodium Metabisulphate and lipolytic enzyme.
- Complete removal of lipids from the lens is achieved by using a stabilised enzyme in fluid form and this may be applied either separately or as a second step. This is typically dripped onto the contact lens so as to remove any lipid deposits.
- the stabilised enzyme in fluid form is, as described above, preferably a lipase with a phosphate buffer.
- a further step in the cleaning operation involves rinsing the contact lens in a physiological saline solution and then boiling the lens in the same or a similar solution.
- the saline solution sould be particle-free (i.e. have a particle size below 0.2 micron), should be isotonic, should have a pH-value of 7.0 and buffer capacity of 6-8 and should also be sterile.
- the pH-value which is indicated is that value which will avoid smarting when the lens is subsequently inserted. An incorrect pH-value will cause smarting to occur. An incorrect pH-value will also cause the protein in the tear fluid to become denatured spontaneously which is not, of course, desirable.
- the solution is preferably packed in a disposable pack and is sterilised by means of Gamma radiation.
- the fluid consists of Lysozyme, Ig y-gobulin, 1-lipoprotein, small amounts of carbohydrates and phospholipids.
- a similar solution was therefore prepared from the following:- y-chymotrypsin, serum albumin, lysozyme, bovine mucin, globulin II, A-globulin III, globulin and A-lipoprotein in 0.9% NaCI solution. Lenses were placed in this prepared solution and left over night. Control lenses were kept in a sterile saline solution instead of the prepared solution. At the end of the period of storage the lenses were divided into four groups:-
- the invention allows soft contact lenses to be cleaned rapidly and effectively and in general the cleaning operation should be carried out daily. However, where lenses are worn day and night, the interval between cleanings may be extended to every other or even every third day.
- the invention therefore provides for a simpler cleaning process than the known technique which requires the dissolving of tablets in water and also provides for a shorter cleaning period than hitherto. What is more important, however, is that the invention allows a more complete cleaning of the contact lens on account of the higher enzymatic activity. Unlike previously known cleaning preparations, the method according to the present invention is also designed to be used daily on the one hand for cleaning the lenses and on the other hand as a preventative measure to prevent the build-up of larger deposits of protein and lipids which after a time are difficult to remove and affect the properties of the lens.
- the types of enzymes which can be utilised may be Papain or Bromelain in each case together with a lipolytic enzyme. Cysteine and Polysaccharides may be used as substrate materials.
- Enzymatic activity should be of the order of 100 tyrosine units per p g of protein (substrate).
- the albumin By splitting the albumin into water-soluble peptones by enzymatic action, the latter can be rinsed or boiled away using a physiological saline isotonic solution.
- the invention provides a stable liquid cleaning agent for cleaning soft contact lenses which can be stored under normal environmental conditions without loss of enzymatic activity thereby obviating the need to dissolve a tablet or quantity of powder in water so as to produce the cleaning solution for the lens.
- the invention provides for the application of the cleaning liquid by means of droplet applicator or the like.
- the Prolen solution described above is used as a regular daily cleaning agent. This will remove most of the deposits normally found on the lens but will not completely remove the Lipid deposits.
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Eyeglasses (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
SE7804614A SE411152B (sv) | 1978-04-21 | 1978-04-21 | Sett att rengora mjuka kontaktlinser |
SE7804614 | 1978-04-21 | ||
GB3887378 | 1978-10-02 | ||
GB7838873A GB2019721B (en) | 1978-04-21 | 1978-10-02 | Method and materials for cleaning soft contact lenses |
Publications (3)
Publication Number | Publication Date |
---|---|
EP0005131A2 EP0005131A2 (en) | 1979-10-31 |
EP0005131A3 EP0005131A3 (en) | 1979-11-28 |
EP0005131B1 true EP0005131B1 (en) | 1983-05-18 |
Family
ID=26269028
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP79850032A Expired EP0005131B1 (en) | 1978-04-21 | 1979-04-23 | Methods and materials for cleaning soft contact lenses |
EP79900454A Withdrawn EP0015968A1 (en) | 1978-04-21 | 1979-11-19 | Methods and materials for cleaning soft contact lenses |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP79900454A Withdrawn EP0015968A1 (en) | 1978-04-21 | 1979-11-19 | Methods and materials for cleaning soft contact lenses |
Country Status (7)
Country | Link |
---|---|
EP (2) | EP0005131B1 (enrdf_load_stackoverflow) |
JP (1) | JPS55500262A (enrdf_load_stackoverflow) |
CH (1) | CH643663A5 (enrdf_load_stackoverflow) |
DE (1) | DE2965421D1 (enrdf_load_stackoverflow) |
FI (1) | FI791296A7 (enrdf_load_stackoverflow) |
NO (1) | NO153107C (enrdf_load_stackoverflow) |
WO (1) | WO1979000963A1 (enrdf_load_stackoverflow) |
Families Citing this family (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4521254A (en) * | 1981-02-09 | 1985-06-04 | Anderson Ronald L | Cleaning contact lenses with solution of bromelain and carboxypeptidase |
EP0093784B1 (de) * | 1982-04-23 | 1987-08-05 | Dr. Thilo & Co. GmbH | Enzymatisches Reinigungsmittel für Kontaktlinsen mit pH-kontrollierter Wirkung |
IE55711B1 (en) | 1983-10-24 | 1990-12-19 | Bausch & Lomb | Improved method for enzymatic cleaning and disinfecting contact lenses |
US4614549A (en) * | 1983-10-24 | 1986-09-30 | Bausch & Lomb Incorporated | Method for enzymatic cleaning and disinfecting contact lenses |
US4690773A (en) * | 1983-10-24 | 1987-09-01 | Bausch & Lomb Incorporated | Microbial enzymatic contact lens cleaner and methods of use |
CA1231069A (en) * | 1983-10-24 | 1988-01-05 | Bausch & Lomb Incorporated | Microbial enzymatic contact lens cleaner and methods of use |
JPS62913A (ja) * | 1985-06-26 | 1987-01-06 | Lion Corp | コンタクトレンズ用洗浄剤 |
GB8629538D0 (en) † | 1986-12-10 | 1987-01-21 | Unilever Plc | Enzymatic dishwashing & rinsing composition |
GB8816443D0 (en) * | 1988-07-11 | 1988-08-17 | Albright & Wilson | Liquid enzymatic detergents |
JPH01180515A (ja) * | 1988-01-13 | 1989-07-18 | Tome Sangyo Kk | コンタクトレンズ用洗浄液及び洗浄方法 |
HU209538B (en) * | 1990-05-09 | 1994-07-28 | Vepex Contractor Ltd | Set and cleaning composition for treating contactlenses |
KR920007641A (ko) * | 1990-10-25 | 1992-05-27 | 스기우라 켄이찌 | 콘택트렌즈용 용액 |
GR1001126B (el) * | 1991-10-09 | 1993-04-28 | Tsakas Spyros Lavipharm Ae | Κα?άρισμα-αποστείρωση φακών επαφής μέσω νέας ενζυμικής και τεχνικής με?οδολογίας. |
ES2114305T3 (es) * | 1993-12-29 | 1998-05-16 | Bausch & Lomb | Composicion a base de glucidos y procedimiento de limpieza y de desinfeccion de lentes de contacto. |
RU2166785C1 (ru) * | 2000-03-17 | 2001-05-10 | ЗАО "Диафарм" | Очищающий раствор для контактных линз |
US20190382685A1 (en) | 2017-01-20 | 2019-12-19 | Albert Sturm | Contact lens cleaning agent |
WO2023101046A1 (ko) * | 2021-12-01 | 2023-06-08 | 주식회사 휴메디솔 | Mpc와 프로테아제 기반의 콘택트렌즈 세정액 및 이의 제조방법 |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3855142A (en) * | 1971-07-15 | 1974-12-17 | Lever Brothers Ltd | Enzymatic denture cleanser |
US3910296A (en) * | 1973-04-20 | 1975-10-07 | Allergan Pharma | Method of removing proteinaceous deposits from contact lenses |
US4096870A (en) * | 1977-06-09 | 1978-06-27 | Burton, Parsons And Company, Inc. | Method for cleaning soft hydrophilic gel contact lenses |
-
1979
- 1979-04-20 JP JP50072079A patent/JPS55500262A/ja active Pending
- 1979-04-20 CH CH1153779A patent/CH643663A5/de not_active IP Right Cessation
- 1979-04-20 FI FI791296A patent/FI791296A7/fi not_active Application Discontinuation
- 1979-04-20 NO NO791335A patent/NO153107C/no unknown
- 1979-04-20 WO PCT/SE1979/000097 patent/WO1979000963A1/en unknown
- 1979-04-23 DE DE7979850032T patent/DE2965421D1/de not_active Expired
- 1979-04-23 EP EP79850032A patent/EP0005131B1/en not_active Expired
- 1979-11-19 EP EP79900454A patent/EP0015968A1/en not_active Withdrawn
Also Published As
Publication number | Publication date |
---|---|
FI791296A7 (fi) | 1981-01-01 |
CH643663A5 (de) | 1984-06-15 |
NO153107B (no) | 1985-10-07 |
EP0005131A3 (en) | 1979-11-28 |
WO1979000963A1 (en) | 1979-11-15 |
NO153107C (no) | 1986-01-15 |
JPS55500262A (enrdf_load_stackoverflow) | 1980-05-01 |
DE2965421D1 (en) | 1983-07-07 |
NO791335L (no) | 1979-10-23 |
EP0005131A2 (en) | 1979-10-31 |
EP0015968A1 (en) | 1980-10-01 |
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