US3644084A - Treatment of keratin fibers - Google Patents

Treatment of keratin fibers Download PDF

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Publication number
US3644084A
US3644084A US778797A US3644084DA US3644084A US 3644084 A US3644084 A US 3644084A US 778797 A US778797 A US 778797A US 3644084D A US3644084D A US 3644084DA US 3644084 A US3644084 A US 3644084A
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solution
keratin
disulfide
fibers
hair
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Du Yung Hsiung
Leszek January Wolfram
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Gillette Co LLC
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Gillette Co LLC
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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q5/00—Preparations for care of the hair
    • A61Q5/04—Preparations for permanent waving or straightening the hair
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/40—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing nitrogen
    • A61K8/44—Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof
    • A61K8/447—Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof containing sulfur
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/46—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing sulfur

Definitions

  • ABSTRACT Keratin fibers are softened by sulfitolysis which forms S-sulfo groups or a mixture of S-sulfo groups with thiol groups in the fibers, then changed in configuration and maintained in the new configuration while restoring the fibers by treating with an aqueous solution containing at pH 5 to l 1 from 0.02 to 0.3 mole per liter of an alkali metal, ammonium or lower alkanolamine sulfide or hydrosulfide, an aliphatic mercaptan, or mixtures thereof with each other or with an aliphatic disulfide.
  • An aliphatic disulfide may be used alone when the ratio of S- sulfo groups to thiol groups in the sulfitolyzed keratin fibers is from 4:1 to 1:4.
  • This invention relates to the treatment of keratin fibers and pertains more specifically to the restoration of sulfitolyzed keratin fibers.
  • the disulfide crosslinkages of keratin are ruptured during chemical setting processes such as the permanent waving of hair, or the permanent creasing or pleating of wool fabrics or garments. Such processes may be considered as consisting of three steps:
  • the most important bonds ruptured in the first step are the disulfide crosslinkages between the polypeptide chains, resulting from the incorporation of the diamino-dicarboxylic acid cystine in the structure:
  • rupture of the keratin disulfide linkage by sulfitolysis is preferable to reduction, on account of the freedom of these reagents from odor and from metal staining problems, and of the greater stability in storage of the ruptured keratin made in this way.
  • the sulfitolysis is believed to occur according to the following equations, with the generation of one S-sulfo group (K-S-SO and one thiol group (K-SH or K-Slfrom each disulfide linkage:
  • the first consists of the use of an oxidant, such as any of those commonly employed for rebuilding reduced keratin. Under normal reaction conditions, these oxidants do not react with S-sulfo groups. Consequently, only the thiol groups are relinked to form disulfide crosslinkages. The S-sulfo groups, which are retained in the rebuilt keratin, tend to swell and weaken the structure by virtue of their hydration and ionization over the whole pH range from pH 1 upward. Hence, the physical and mechanical properties of the .fiber are not completely restored, the fiber being weak and rubbery when wet, and brittle and hard in the dry state.
  • an oxidant such as any of those commonly employed for rebuilding reduced keratin.
  • the second way of rebuilding disulfide linkages in sulfitolyzed keratin consists in reversing the sulfitolysis reactions, which are equilibrium reactions, by removal of sulfite or bisulfite reactant, for example by rinsing the keratin fiber with water.
  • This process is inefficient because the sulfite and bisulfite ions are strongly sorbed by keratin, so that their complete removal by rinsing is difficult; unfortunately, the presence of only a small quantity of either ion suffices to maintain a substantial extent of disulfide bond rupture.
  • the third method by which partial rebuilding can be accomplished consists in changing the pH of the keratin fiber. Because the extent to which the sulfitolysis reactions proceed before reaching equilibrium varies depending upon the pH of the reaction, reaching a maximum at about pH 6, if the sulfitolysis is carried out at this pH and is allowed to approach equilibrium, some disulfide linkages can be restored by appropriate change in pH, usually upward from 6.
  • the second and the third methods just described are frequently employed in conjunction.
  • the sulfitolysis of keratin fibers during the process of the present invention can be carried out in any conventional manner.
  • the fibers may be brought into contact with an aqueous solution of such sulfitolyzing agents as watersoluble sulfites, bisulfites or hydrosulfites, for example the alkali metal or ammonium or lower alkanolamine salts. Solutions containing 0.1 to 4.0 moles or more of the sulfitolysis ingredient per liter may be used.
  • the ratio of S-sulfo groups to thiol groups in the sulfitolyzed hair is approximately lzl, as indicated by equations l
  • an oxidizing agent such as a transition metal ion in the higher oxidation state such as cupric of ferric ion, or such as a watersoluble polythionate as described in the copending application of Wolfram, Ser. No. 488,759 filed Sept. 20, 1965 now abandoned.
  • Such polythionates include the alkali metal, ammonium, or lower alkanolamine trithionates, tetrathionates, pentathionates and hexathionates; they may be present in amounts from 0.05 to 2 moles or more per liter.
  • an oxidizing agent When sulfitolyzation is carried out in the presence of such an oxidizing agent the ratio of S-sulfo groups to thiol groups in the sulfitolyzed hair is greater than 1:1, if sufficient oxidizing agent is employed the ratio is greatly increased, approaching the point where the sulfitolyzed hair contains only S-sulfo groups and no thiol groups.
  • sulfitolyzation may be carried out by using solutions containing in addition to sulfites, bisulfites or hydrosulfites a reducing agent such as a water-soluble mercaptan, including any of those hereinafter described for use in restoring the disulfide linkages.
  • a reducing agent such as a water-soluble mercaptan
  • Such sulfitolyzing solutions may have a pH from 4.5 to l l, the pH being adjusted by the addition of ammonia or other a1 kaline material or of conventional buffer salts. It will be understood that there may also be present in the sulfitolyzing composition conventional protein swelling agents such as urea, isopropanol, lithium bromide, phenol and the like in amounts up to 8 moles per liter, or deswelling agents such as various inert water-soluble salts, e.g., sodium chloride, potassium chloride, sodium sulfate, magnesium sulfate and the like, in amounts up to 1 mole per liter.
  • conventional protein swelling agents such as urea, isopropanol, lithium bromide, phenol and the like in amounts up to 8 moles per liter
  • deswelling agents such as various inert water-soluble salts, e.g., sodium chloride, potassium chloride, sodium sulfate, magnesium sulfate and the like
  • the sulfitolytic solution may be applied to hair on the human head in the same ways as waving or straightening lotions are conventionally applied.
  • the fibers or fabric may simply be immersed in the solution, or the solution may be applied by various other conventional methods such as by padding.
  • the temperature of the solution may be from room temperature (20 C.) to as high as the boiling point (ca. 100 C.), but when the solution is used as a waving lotion on the human head the temperature of the solution normally does not exceed about 50 C.
  • the time required to effect substantial sulfitolysis varies depending upon the temperature and concentration of the solution, as is well known; usually the solution should be left on the hair for at least 10 minutes at room temperature but at a temperature as high as the boiling point, which may be used in the case of wool, substantial sulfitolysis occurs during treatment which lasts only a few seconds.
  • the relative proportion of S-sulfo groups and of thiol groups in sulfitolyzed hair can readily be determined by analysis of three fresh samples, each weighing about 0. l-O.2 gram, by the following methods.
  • the first sample after blotting with a towel, is washed by immersion in three successive 25 ml. portions of 6 normal sulfuric acid at room temperature for periods of 1 minute, 1 minute, and 14 minutes successively, then hydrolyzed by heating for 17 hours at 95 C. in approximately 85 ml. of 6 normal sulfuric acid.
  • the hydrolysis converts each mole of S-sulfo keratin to 1 mole of cysteine.
  • the mixture is then cooled to room temperature, diluted with water to ml.
  • cysteine present is determined by titration. This includes both the cysteine formed by acid hydrolysis of the S-sulfo keratin and the cysteine formed along with the S-sulfo keratin in the sulfitolysis process of equation (1).
  • the aliquot of acid hydrolysate to be titrated is first alkalized with an excess of sodium carbonate and then titrated with an aqueous solution which is 0.1 N in salyrganic acid and 1.0 N in sodium chloride, using a 1 percent aqueous solution of sodium nitroprusside as the indicator.
  • the results are expressed as millimoles/gram of hair sample of the total of both S-sulfo and thiol groups, designated MNP
  • MNP millimoles/gram of hair sample of the total of both S-sulfo and thiol groups
  • the sample is subjected to the 17-hour sulfuric acid hydrolysis step and to titration as in the case of the first two samples.
  • the results are expressed as millimoles per gram of sample of residual S-sulfo groups after reversal, designated MNP From the foregoing, the millimoles of S-sulfo group per gram oforiginal sample can be calculated as follows:
  • the excess sulfitolysis solution is removed from the fibers as by rinsing with water and there is then applied to the fibers an aqueous solution comprising the desired sulfur-containing compounds.
  • the water-soluble compounds which may be used include the alkali metal, ammonium, and lower alkanolamine sulfides and hydrosulfides as well as the water-soluble aliphatic mercaptans and aliphatic disulfides as well as mixtures.
  • lower alkanolamines is meant mono-, di-, and triethanolamine, and mono-, di-, and tri-isopropanolamine.
  • water-soluble mercaptans are cysteine, thio-glycolic acid, dimercaptoadipic acid, thiolactic acid, beta-mercaptopropionic acid, thioglycol, thioglycerol, and mercaptoethyl sulfonate; in general open chain aliphatic mercaptans containing not over six carbon atoms and containing one or more hydroxyl groups, amino groups or acidic groups, such as carboxylic or sulfonic are satisfactory.
  • the useful disulfides include those corresponding to the foregoing mercaptans, for example, cysteine, dithiodiglycolic acid, the cyclic disulfide of dimercaptoadipic acid, the disulfide of thiolactic acid, the disulfide of beta-mercaptopropionic acid, and the like.
  • the process of the present invention is concerned only with sulfitolyzed hair in which the ratio of S-sulfo groups to thiol groups is 1:4 or greater, up to and including such hair in which no thiol groups but only S-sulfo groups are present.
  • hair ranges from 4:1 to 1:4.
  • the aliphatic disulfide is 1 used in admixture with the sulfides or hydrosulfides or mercaptans, however, the mixture may be used over the entire range from 100 percent S-sulfo groups down to as low as a ratio of 1:4 S-sulfozthiol groups.
  • disulfide reacts with a keratin thiol group to generate mixed disulfide and a mercaptan:
  • the mercaptan so generated is available to reform one disulfide crosslinkage from two keratin S-sulfo groups, and to form 1 mole of sulfite, as explained above in reaction (4); the sulfite then reacts with the unstable mixed disulfide arising from reaction (6), either a keratin thiol group or a keratin S-sulfo group being liberated; it is believed, according to the following reactions:
  • Rebuilding of disulfide crosslinkages then proceeds according to the reverse of reaction (1).
  • the rebuilding may be promoted by removal of the sulfite from reaction l
  • elevation of pH is helpful, as the higher the pH, the farther to the left lies the equilibrium in reaction (1).
  • the reagent concentration may be selected in any given case on the basis of extent and rate of rebuilding desired, economics, and similar factors. In general, there is no advantage in using a concentration of disulfide above 1.0 molar. When a disulfide is present, it is usually desirable that it amount to at least 0.02 molar.
  • the pH of the solution of sulfur-containing compounds may vary from 5 to l 1, although it is preferred that it be maintained from 6 to for solutions to be used in restoring sulfitolyzed wool, and that it be maintained from 5 to 9 in solutions to be used on hair. For best results the pH of the solution should be maintained from 7 to 9 in every case.
  • the carboxylic groups present in certain aliphatic mercaptans and disulfides may be in the form of carboxylate groups, e.g., ammonium carboxylate, in the case of those solutions in the higher pH range.
  • the amount of sulfur-containing compound present in the aqueous solution, exclusive of disulfide present, may vary over a wide range from 0.02 to about 0.3 mole per liter.
  • the aqueous solution of the sulfur-containing compound may be applied to the keratin fibers in the same manner as the sulfitolyzing solution is conventionally applied. While the temperature of the solution may be above 35 C., even as high as 50 C., in some cases as for example in the case of wool, it is generally preferred to maintain the temperature no higher than 35 C., particularly in applying the solution to hair on a human head.
  • the solution of the sulfur-containing compound For effective restoration of sulfitolyzed hair, the solution of the sulfur-containing compound must be maintained in contact with the hair fibers for at least about 5 minutes at room temperature. While a period of 30 minutes usually suffices to ensure complete restoration of the hair fibers, there are no adverse effects from maintaining the solution in contact with the hair for longer periods of time.
  • the fibers may simply be washed with water and dried.
  • the sulfur-containing compound is an aliphatic mercaptan
  • a conventional neutralizing agent of the type used in hair waving.
  • Such solutions contain conventional oxidizing agents such as peroxides, bromates, perborates, percarbonates, and the like which serve to oxidize any excess mercaptan sorbed in the fibers or incompletely removed during the rinsing step.
  • EXAMPLE 1 Bundles of brown European hair fibers 10 inches long were immersed in water at 30 C. for 1 hour. The modulus of the hair was measured by stretching the bundle of hair between two supports so that the bundle was extended by 1 percent of its length, then measuring the force required to produce an additional extension of 0.2 percent of the length of the bundle.
  • EXAMPLE 2 The same procedure was employed as in Example 1 except that the sulfitolyzing solution was adjusted to pH 6 with ammonia rather than to pH 9.5, which produced approximately the same ratio of S-sulfo groups to thiol groups.
  • the aqueous solutions of sulfur-containing compounds contained only ammonium thioglycolate adjusted to pH 8 at varying concentrations. The effectiveness of these solutions in restoring the keratin is shown by the measurement of relative modulus as set forth in the following table.
  • Measurements of extent of swelling of the hair fibers and analysis of the hair fibers for cysteine content also show the great effectiveness of the method of the present invention for restoring the fibers after sulfitolysis to a condition similar to that of untreated hair.
  • EXAMPLE 3 Samples of brown European hair, 1 gram in weight, were immersed in an aqueous solution lM in ammonium bisulfite and 0.2M in potassium trithionate, adjusted to pH 7 by means of ammonia, at 35 C. for 30 minutes. They were then rinsed for l minute in deionized water at which point they contained S-sulfo groups and thiol groups in a ratio of about 19: l. Each of the samples was immersed for 15 minutes in one of several different rebuilding solutions, all of which were adjusted to pH 7, at 35 C. The rebuilding solutions used included cysteine at concentrations of 0.004M, 0.0l6M, and 0.1M, and sodium hydrosulfide at 0.1M. The samples were then rinsed with water.
  • Portions of the samples were equilibrated with an atmosphere of 65 percent relative humidity; one portion was analyzed for thiol content, and another for total sulfur content.
  • EXAMPLE 4 Tresses of brown European human hair, 5 inches long, weighing 1 g. each, and having the fibers glued to plastic tabs at their rootward ends, were shampooed, and then saturated with a solution 1M in ammonium bisulfite, 3M in urea, which had its pH adjusted to 7.0 by means of ammonia. The tresses were then wound on waving rods, placed on a flat surface maintained at 35 C., and covered with a plastic sheet. After minutes, the tresses were resaturated with the same solution, and the treatment was allowed to continue for a further 15 minutes; the wound tresses were then rinsed with warmrunning tap water for 2 minutes.
  • the tresses were wetted out and rated for degree of curl impartation by comparison with a graded series of photographs on which grade 1 represents completely straight hair, and grade 10 an excessive amount of curl; they were then wound on setting rollers of A-inch diameter, and allowed to dry at room temperature overnight. At this point they were unwound, suspended in an atmosphere of 65 percent relative hu- Set-Holding, cm.
  • the physico-chemical characteristics of the hair treated in accordance with the present invention are greatly superior to the characteristics of hair treated with hydrogen peroxide solution.
  • an aliphatic disulfide viz: ammonium dithiodiglycolate
  • Hair treated with the solution of the disulfide not only displayed set-holding characteristics superior to the hair treated with hydrogen peroxide but also displayed superior resistance to dissolution in alkali and to swelling in thioglycolate solution.
  • EXAMPLE 5 Tresses about 3 inches long were prepared from Negro hair from female heads in the manner described in Example 3. After thorough shampooing with a solution of nonionic detergent, each tress was saturated with a solution 1M in ammonium bisulfite and 3M in urea, adjusted to pH 7.0 by means of ammonia, and thickened by the addition of 1 percent ofa guar gum thickener.
  • the tresses were then placed on a flat surface maintained at 33 C., and covered with a plastic sheet. After 15 minutes, the plastic sheet was removed, the tresses were resaturated with the solution, and then periodically combed for the next l5 minutes. The treatment was concluded by a 2-minute running tap water rinse, resulting in a ratio of S-sulfo groups to thiol groups in the hair of approximately 1:1. Thereafter, duplicate tresses were saturated, by combing on, with the solutions shown in the table below, which were allowed to remain in contact with the hair for 5 minutes before rinsing, shampooing and air-drying.
  • the hair was then rated for degree of curl removal, using a subjective scale on which 5" represents complete straightening, and 0 no straightening, by three skilled observers.
  • EXAMPLE 6 An undyed wool-worsted flannel, of plain weave construction, weighing oz./sq. yd., was cut into rectangular swatches 5 inches long in the filling and inches long in the warp direction.
  • the swatches were immersed for 5 minutes, at 25 C., in an aqueous solution 0.2M in sodium bisulfite, 1M in urea, adjusted to pH 7 by means of sodium hydroxide and containing 0.01 percent of a nonionic wetting agent.
  • the ratio of weight of fabric to volume of reagent solution was 20:1.
  • the sulfitolyzed wool fibers contained S-sulfo groups and thiol groups in a ratio of approximately lzl.
  • the method of treating keratin fibers which comprises first reacting the fibers with a first aqueous solution containing a member of the group consisting of water-soluble sulfites, bisulfites, and hydrosulfites to form S-sulfo groups and thiol groups in a ratio of at least 1:4 in the keratin or to form S-sulfo groups alone in the keratin, removing the excess of said first solution changing the configuration of the fibers, and subsequently bringing said keratin fibers while maintained in changed configuration into contact with a second aqueous solution comprising from 0.02 to about 0.3 mole per liter of a water-soluble sulfur-containing compound selected from the group consisting of alkali metal, ammonium, and lower alkanolamine sulfides; alkali metal, ammonium and lower alkanolamine hydrosulfides; aliphatic mercaptans; and mixtures thereof with each other and with aliphatic disulfides; at
  • the method of treating keratin fibers which comprises first reacting the fibers with a first aqueous solution containing a member of the group consisting of water-soluble sulfites, bisulfites, and hydrosulfites to form a mixture of S-sulfo groups and thiol groups in a ratio of 4:1 to 1:4 in the keratin, removing the excess of said first solution, and changing the configuration of the fibers, and subsequently bringing said keratin fibers while maintained in changed configuration into contact with a second aqueous solution comprising from 0.02 to about 0.3 mole per liter of a water-soluble aliphatic disulfideatapl-lofS to 11.
  • the keratin fibers comprise human hair
  • the sulfur-containing compound comprises an aliphatic mercaptan in an amount from 0.02 to 0.3 mole per liter
  • the pH of said second solution is 7 to 8
  • the temperature of said second solution is from room temperature to 35 C.

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US778797A 1968-11-25 1968-11-25 Treatment of keratin fibers Expired - Lifetime US3644084A (en)

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JP (1) JPS523039B1 (enrdf_load_stackoverflow)
BE (1) BE742085A (enrdf_load_stackoverflow)
DE (1) DE1959149A1 (enrdf_load_stackoverflow)
FR (1) FR2024206A1 (enrdf_load_stackoverflow)
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Cited By (17)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5294230A (en) * 1986-07-11 1994-03-15 The Gillette Company Method for permanent waving and straightening of hair
US5565192A (en) * 1993-05-25 1996-10-15 L'oreal Process for the permanent-reshaping of hair and composition for carrying it out containing, in combination, an amino- or amidothiol and at least one inorganic bromide
US20030169769A1 (en) * 2002-03-08 2003-09-11 Texas Instruments Incorporated MAC extensions for smart antenna support
EP1406918A4 (en) * 2001-07-17 2005-04-06 Keratec Ltd PREPARATION OF SOLUBLE KERATIN DERIVATIVES
US20060165635A1 (en) * 2002-11-28 2006-07-27 Kelly Robert J Personal care formulations containing keratin
US20070065506A1 (en) * 2005-03-11 2007-03-22 Kelly Robert J Keratin and soluble derivatives thereof for a nutraceutical and to reduce oxidative stress and to reduce inflammation and to promote skin health
US20080004423A1 (en) * 2003-09-19 2008-01-03 Robert James Kelly Composite Materials Containing Keratin
US20080039951A1 (en) * 2002-06-10 2008-02-14 Keratec Limited Orthopaedic materials derived from keratin
US20080038327A1 (en) * 2003-12-19 2008-02-14 Robert James Kelly Wound Care Products Containing Keratin
US20080206301A1 (en) * 2006-12-06 2008-08-28 Robert James Kelly Bone void fillers and methods of making the same
US7465321B2 (en) 2001-08-31 2008-12-16 Keratec Limited Production of biopolymer film, fibre, foam and adhesive materials from soluble S-sulfonated keratin derivatives
US20080317826A1 (en) * 2007-05-24 2008-12-25 Robert James Kelly Porous keratin constructs, wound healing assemblies and methods using the same
US20090105456A1 (en) * 2006-12-11 2009-04-23 Robert James Kelly Porous keratin construct and method of making the same
US20090111750A1 (en) * 2007-10-31 2009-04-30 Keratec, Ltd. Keratin derivatives and methods of making the same
WO2010114938A1 (en) * 2009-03-31 2010-10-07 Keraplast Technologies, Ltd. Soluble hydrolyzed keratin production
US9045600B2 (en) 2009-05-13 2015-06-02 Keraplast Technologies, Ltd. Biopolymer materials
WO2016174367A1 (fr) 2015-04-30 2016-11-03 Carlini Rosanna Complexe protéomélanique bioassimilable, préparation et utilisations

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS556377U (enrdf_load_stackoverflow) * 1978-06-29 1980-01-16
JPS5540115U (enrdf_load_stackoverflow) * 1978-09-08 1980-03-14
JPS5647169U (enrdf_load_stackoverflow) * 1979-09-21 1981-04-27
EP0236533A1 (en) * 1984-09-14 1987-09-16 Sumitomo Pharmaceuticals Company, Limited Permanent wave preparation
DE3781626T2 (de) * 1986-07-11 1993-04-15 Gillette Co Verfahren und mittel zum dauerwellen und -strecken der haare.
AUPM885294A0 (en) * 1994-10-17 1994-11-10 Commonwealth Scientific And Industrial Research Organisation Chemically assisted protein annealing treatment
KR102234179B1 (ko) 2013-03-27 2021-03-31 가부시끼 가이샤 구보다 콤바인

Cited By (23)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5294230A (en) * 1986-07-11 1994-03-15 The Gillette Company Method for permanent waving and straightening of hair
US5565192A (en) * 1993-05-25 1996-10-15 L'oreal Process for the permanent-reshaping of hair and composition for carrying it out containing, in combination, an amino- or amidothiol and at least one inorganic bromide
EP1406918A4 (en) * 2001-07-17 2005-04-06 Keratec Ltd PREPARATION OF SOLUBLE KERATIN DERIVATIVES
US7465321B2 (en) 2001-08-31 2008-12-16 Keratec Limited Production of biopolymer film, fibre, foam and adhesive materials from soluble S-sulfonated keratin derivatives
US20030169769A1 (en) * 2002-03-08 2003-09-11 Texas Instruments Incorporated MAC extensions for smart antenna support
US7892572B2 (en) 2002-06-10 2011-02-22 Keraplast Technologies, Ltd. Orthopaedic materials derived from keratin
US20080039951A1 (en) * 2002-06-10 2008-02-14 Keratec Limited Orthopaedic materials derived from keratin
US20060165635A1 (en) * 2002-11-28 2006-07-27 Kelly Robert J Personal care formulations containing keratin
US20080004423A1 (en) * 2003-09-19 2008-01-03 Robert James Kelly Composite Materials Containing Keratin
US7767756B2 (en) 2003-09-19 2010-08-03 Keraplast Technologies, Ltd. Composite materials containing keratin
US7732574B2 (en) 2003-12-19 2010-06-08 Keraplast Technologies, Ltd. Wound care products containing keratin
US20080038327A1 (en) * 2003-12-19 2008-02-14 Robert James Kelly Wound Care Products Containing Keratin
US7579317B2 (en) 2005-03-11 2009-08-25 Keratec, Ltd. Nutraceutical composition comprising soluble keratin or derivative thereof
US20070065506A1 (en) * 2005-03-11 2007-03-22 Kelly Robert J Keratin and soluble derivatives thereof for a nutraceutical and to reduce oxidative stress and to reduce inflammation and to promote skin health
US20080206301A1 (en) * 2006-12-06 2008-08-28 Robert James Kelly Bone void fillers and methods of making the same
US8142807B2 (en) 2006-12-06 2012-03-27 Keraplast Technologies, Ltd. Bone void fillers and methods of making the same
US20090105456A1 (en) * 2006-12-11 2009-04-23 Robert James Kelly Porous keratin construct and method of making the same
US8124735B2 (en) 2006-12-11 2012-02-28 Keraplast Technologies, Ltd. Porous keratin construct and method of making the same
US20080317826A1 (en) * 2007-05-24 2008-12-25 Robert James Kelly Porous keratin constructs, wound healing assemblies and methods using the same
US20090111750A1 (en) * 2007-10-31 2009-04-30 Keratec, Ltd. Keratin derivatives and methods of making the same
WO2010114938A1 (en) * 2009-03-31 2010-10-07 Keraplast Technologies, Ltd. Soluble hydrolyzed keratin production
US9045600B2 (en) 2009-05-13 2015-06-02 Keraplast Technologies, Ltd. Biopolymer materials
WO2016174367A1 (fr) 2015-04-30 2016-11-03 Carlini Rosanna Complexe protéomélanique bioassimilable, préparation et utilisations

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NO131177B (enrdf_load_stackoverflow) 1975-01-06
BE742085A (enrdf_load_stackoverflow) 1970-05-25
JPS523039B1 (enrdf_load_stackoverflow) 1977-01-25
FR2024206A1 (enrdf_load_stackoverflow) 1970-08-28
NO131177C (enrdf_load_stackoverflow) 1975-04-16
GB1255365A (en) 1971-12-01
DE1959149A1 (de) 1970-05-27

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