Drug – bio-affecting and body treating compositions – Live hair or scalp treating compositions – Amphoteric or zwitterionic surfactant containing
Patent
1995-12-11
1999-03-09
Wax, Robert A.
Drug, bio-affecting and body treating compositions
Live hair or scalp treating compositions
Amphoteric or zwitterionic surfactant containing
424 941, 424 942, 424 945, 435233, 132210, A61K 709, A61K 3851, C12N 990, A45D 700
Patent
active
058796649
DESCRIPTION:
BRIEF SUMMARY
FIELD OF THE INVENTION
The present invention relates to an active recombinant fungal protein disulfide isomerase, compositions comprising said fungal protein disulfide isomerase, and methods for their use; a DNA construct comprising a DNA sequence encoding said fungal protein disulfide isomerase, and a vector and cell harbouring the DNA construct. Furthermore, the present invention relates to a method of preparing the fungal protein disulfide isomerase by use of both traditional and recombinant DNA techniques.
BACKGROUND OF THE INVENTION
The use of protein disulfide redox agents such as protein disulfide isomerases (PDI), and thioredoxins (TRX) for various purposes has been known for some time.
Protein disulfide redox agents catalyse the general reaction: +Enz.sub.red (reaction I) different, either within the same polypeptide or in two polypeptides, Enz.sub.ox is a protein disulfide redox agent in the oxidised state, and Enz.sub.red is a protein disulfide redox agent in the reduced state. EC 5.3.4.1 refers to an enzyme capable of capable of catalysing the rearrangement of --S--S-- bonds in proteins and EC 1.6.4.4 and EC 1.8.4.2 is an example of enzymes catalysing the reaction with NAD(P)H and glutathione as a mediator, respectively.
This type of activity has been designated as protein disulfide isomerase, sulfhydryl oxidase, protein disulfide reductase, disulfide isomerase, protein disulfide transhydrogenase, and sulfhydryl oxidase.
Disulfide linkages in proteins are formed between cysteine residues and have the general function of stabilising the three dimensional structure of the proteins. They can be formed between cysteine residues of the same or different polypeptides.
Disulfide linkages are present in many types of proteins such as enzymes, structural proteins, etc. Enzymes are catalytic proteins such as proteases, amylases, etc., while structural proteins can be scleroproteins such as keratin, etc. Protein material in hair, wool, skin, leather, hides, food, fodder, stains, and human tissue contains disulfide linkages. Treatment of some of these materials with PDI and TRX, and a redox partner have been described previously.
The use of TRX for waving, straightening, removing and softening of human and animal hair was described by Pigiet et al. (EP 183506 and WO 8906122). Pigiet (U.S. Pat. No. 4,771,036) also describes the use of TRX for prevention and reversal of cataracts. Schreiber (DE 2141763 and DE 2141764) describes the use of protein disulfide transhydrogenase for changing the form of human hair. Pigiet (EP 225156) describes the use of TRX for refolding denatured proteins. Use of TRX to prevent metal catalysed oxidative damage in biological reactions is described by Pigiet et al. (EP 237189).
Toyoshima et al. (EP 277563 and EP 293793) describes the use of PDI to catalyse renaturation of proteins having reduced disulfide linkages or unnatural oxidised disulfide linkages, in particular in connection with renaturation of recombinantly produced proteins. Brockway (EP 272781), and King and Brockway (EP 276547) describe the use of PDI for reconfiguration of human hair, and for treatment of wool, respectively. Sulfhydryl oxidase for the treatment of Ultra-high temperature sterilized milk is described in U.S. Pat. No. 4,894,340, U.S. Pat. No. 4,632,905, U.S. Pat. No. 4,081,328 and U.S. Pat. No. 4,053,644. Schreiber (DE 2141763 and DE 2141764) describes the use of protein disulfide transhydrogenase for changing the form of human hair.
The uses of such enzymes have all been connected with reduction of protein disulfide linkages to free protein sulhydryl groups and/or the oxidation of protein sylfhydryl groups to protein disulfide linkages, and/or the rearrangement of disulfide linkages in the same or between different polypeptides, and sometimes to the use of these processes in sequence.
Protein disulfide redox agents can be divided into two main groups of enzymes, thioredoxin type (TRX), and protein disulfide isomerase type (PDI).
Both these can be modified to obtain protein engineered derivatives, c
REFERENCES:
patent: 4894340 (1990-01-01), Hammer et al.
patent: 5496719 (1996-03-01), Yamada et al.
Mizunaga et al. (1990) Purification and characterization of yeast protein disulfide isomerase. J. Biochm. 108: 846-851, Jan. 1990.
Lundstrom et al. (1992) A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. J. Biol. Chem. 267 (13): 9047-9052, May 1992.
Rudinger (1976) Characteristics of the amino acids as components of a peptide hormone sequence. In: Peptide Hormones. Ed. J. A. Parsons, University Park Press, Baltimore, MD, pp. 1-7, Jun. 1976.
Schreiber (1973) Hair-shaping composition. STN Online, Chemical Abstracts, Columbus, OH, Caplus No. 1973:140360, Mar. 1973.
Miyamoto (1988) Skin cosmetics containing sulfhydryl oxidase and water-soluble polyhydric alcohols. STN Online, Chemical Abstracts, Columbus, OH. Caplus No. 1990:597686, Dec. 1988.
Miyamoto (1989) Hair cosmetic compositions containing sulfhydryl oxidase and water-soluble polyalcohols. STN Online< Chemical Abstracts, Columbus, OH. Caplus No. 1990:637563, Feb. 1989.
Kise et al. (1992) Hair wave-setting oxidizing agents containing enzyme. STN Online, Chemical Abstracts, Columbus, OH. Caplus No. 1992:241716, Apr. 1990.
Sugiyama et al., Biosci. Biotech. Biochem. vol. 57, No. 10, pp. 1704-1707, 1993.
Gregg, Esq. Valeta
Novo Nordisk A S
Stole Einar
Wax Robert A.
Zelson Esq. Steve T.
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