Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Scleroproteins – e.g. – fibroin – elastin – silk – etc.
Reexamination Certificate
2006-02-21
2006-02-21
Wax, Robert A. (Department: 1653)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Scleroproteins, e.g., fibroin, elastin, silk, etc.
C530S350000
Reexamination Certificate
active
07001988
ABSTRACT:
Methods for chemically modifying peptides, preferably keratinaceous feedstocks, to achieve desired solubility characteristics; stable solvent systems for preparing the modified peptides; and, the resulting chemically modified peptides.
REFERENCES:
patent: 922692 (1909-05-01), Goldsmith
patent: 926999 (1909-07-01), Neuberg
patent: 960914 (1910-06-01), Heinemann
patent: 2434688 (1948-01-01), Evans
patent: 3250682 (1966-05-01), Wilmsmann et al.
patent: 3642498 (1972-02-01), Anker
patent: 3677693 (1972-07-01), Fillingham
patent: 3842848 (1974-10-01), Karlala
patent: 4041150 (1977-08-01), Karjala
patent: 4279996 (1981-07-01), Yoshioka et al.
patent: 4423032 (1983-12-01), Abe et al.
patent: 4474694 (1984-10-01), Coco et al.
patent: 4495173 (1985-01-01), Matsunaga et al.
patent: 4504644 (1985-03-01), Lang et al.
patent: 4570629 (1986-02-01), Widra
patent: 4659566 (1987-04-01), Petrow
patent: 4751074 (1988-06-01), Matsunaga et al.
patent: 4895722 (1990-01-01), Abe et al.
patent: 4906460 (1990-03-01), Kim et al.
patent: 4959213 (1990-09-01), Brod et al.
patent: 5047249 (1991-09-01), Rothman et al.
patent: 5073294 (1991-12-01), Shannon et al.
patent: 5202053 (1993-04-01), Shannon
patent: 5219562 (1993-06-01), Fujiu et al.
patent: 5258501 (1993-11-01), Barbaric et al.
patent: 5276138 (1994-01-01), Yamada et al.
patent: 5300285 (1994-04-01), Halloran et al.
patent: 5356433 (1994-10-01), Rowland et al.
patent: 5358935 (1994-10-01), Smith et al.
patent: 5412076 (1995-05-01), Gagnieu
patent: 5424062 (1995-06-01), Schwan et al.
patent: 5425937 (1995-06-01), Uchiwa et al.
patent: 5505952 (1996-04-01), Jiang et al.
patent: 5520925 (1996-05-01), Maser
patent: 5563230 (1996-10-01), Hsu et al.
patent: 5654471 (1997-08-01), Zahn et al.
patent: 5679819 (1997-10-01), Jones et al.
patent: 5712252 (1998-01-01), Smith
patent: 5833880 (1998-11-01), Siemensmeyer et al.
patent: 5932552 (1999-08-01), Blanchard et al.
patent: 5942009 (1999-08-01), Burns
patent: 5948432 (1999-09-01), Timmons et al.
patent: 5955549 (1999-09-01), Chang et al.
patent: 5989461 (1999-11-01), Coates et al.
patent: 6087462 (2000-07-01), Bowers et al.
patent: 6090308 (2000-07-01), Coates et al.
patent: 6110487 (2000-08-01), Timmons et al.
patent: 6124265 (2000-09-01), Timmons et al.
patent: 6159495 (2000-12-01), Timmons et al.
patent: 6159496 (2000-12-01), Blanchard et al.
patent: 6165496 (2000-12-01), Timmons et al.
patent: 6211296 (2001-04-01), Frate et al.
patent: 6270791 (2001-08-01), Van Dyke et al.
patent: 6270793 (2001-08-01), Van Dyke et al.
patent: 6274155 (2001-08-01), Van Dyke et al.
patent: 6274163 (2001-08-01), Blanchard et al.
patent: 6316598 (2001-11-01), Van Dyke et al.
patent: 6352699 (2002-03-01), Mondet et al.
patent: 6361767 (2002-03-01), Malle et al.
patent: 6371984 (2002-04-01), Van Dyke et al.
patent: 6379690 (2002-04-01), Blanchard et al.
patent: 6399051 (2002-06-01), Dannecker et al.
patent: 6432435 (2002-08-01), Timmons et al.
patent: 6435193 (2002-08-01), Cannell et al.
patent: 6461628 (2002-10-01), Blanchard et al.
patent: 2005/0054053 (2005-03-01), Aguinaldo et al.
patent: 0097907 (1984-01-01), None
patent: 0 298 684 (1989-01-01), None
patent: 0454 6000 (1991-10-01), None
patent: 0 468 797 (1992-01-01), None
patent: 0540357 (1993-05-01), None
patent: 57-23631 (1982-02-01), None
patent: 4-189833 (1992-07-01), None
patent: 2002-113815 (2002-04-01), None
patent: WO 93/10827 (1993-06-01), None
patent: WO 93/22397 (1993-11-01), None
patent: WO 98/08550 (1995-03-01), None
patent: WO 9931167 (1999-06-01), None
patent: WO 03008006 (2003-01-01), None
Croda, Ltd., Keratec Pep, DC138—Pep—Datasheet, Apr. 13, 2004.
S. F. Sadova and A. A. Konkin, Grafting of vinyl monomers onto wool keratin in an oxidation-reduction system. Zh Vses Khim O-va 1967; 12(5): 596-7.
Iwata, et al.; Coating Film For Living Tissues; Nov. 2, 1985; total of 9 pages; Japanese Patent Application Kokai Publication No. Sho 60-220068.
Endo; De-Allergenized Rubber of Plastic Molding Used in the Field of Medicla Care; Apr. 16, 2002; total of 5 pages; Japanese Patent Application Kokai Publication No. 2002-113815.
Yoshioka et al; Modified Animal Hair or Wool Powder, Jul. 11, 1989; total of 13 pages; Japanese Unexamined Patent Application Publication H01-174528.
Miyamoto et al; Process for Producing Modified Keratin Protein; Feb. 6, 1982; total of 4 pages; Japanese Patent Application Kokai Publication No. Sho 57-23631.
Yamauchi et al; Karatin Microcapsule, Production of Keratin Microcapsule, and Cosmetics containing Keratin Microcapsules; Dec. 22, 1998; total of 5 pages; japanes Patent Application Kokai Publication No. H10-3337466.
J.M. Gillespie, et al., “Amino Acid composition of a Sulphur-rich Protein Wool,” Biochim. Biophy. ACTA, (1960) pp. 538-539; vol. 39.
Keith H. Gough, et al., “Amino Acid Sequence of alpha -Helical Segments from S-Carboxymethylkerateine-A: Complete Sequence of a Type-I Segment,” Biochem. J. (1978), pp. 373-385; vol. 173.
Thomas C. Elleman, et al., “Amino Acod Sequemces pf alpha -Helical Segments from S-Carboxymethylkerateine-A:. Statistical Analysis,” Biochem. J. (1978), pp. 387-391, vol. 173.
David McC. Hogg, et al., “Amino Acid Sequences of alpha-Helical Segments from S-Carboxymethlkerateine-:. Tryptic and Chymotryptic Peptides from a Type-II Segment,” Biochem. J. (1978), pp. 353-363; vol. 173.
W. Gordon Crewther, et al., “Amino Acid Sequences of alpha -Helical Segments from S-Carboxymethylkerateine-A: Complete Sequence of a Type-II Segment,” Biochem. J. (1978), pp. 405-411. vol. 22.
C. Earland, et al., “Studies on the Structure of Karatin: II. The Amino Acid Context of Fractions Isolated from Oxidized Wool,” Biochemica Et Biophysica Acta (1956), pp. 405-411. vol. 22.
J.M. Gillespie, et al., “Preparation of an Electrophoretically Homogeneous Keratin Derivative from Wool,” Short Communications, Preliminary Notes, (1953), pp. 481-482, vol. 12.
Maurice J. Frenkel, et al., “The Isolation and Properties of a Tyrosine-Rich Protein from Wool: component 0.62,” Eur. J. Biochem, (1973) pp. 112-119, vol. 34.
R.J. Blagrove, et al., “The Electrophoresis of the High-Tyrosine Proteins of Keratins on Cellulose Acetate Strips,” Comp. Biochem. Physiol., (1975) pp. 571-572, vol. 50B.
Robert C. Marshall, et al., “Successful Isoelectric Focusing of Wool Low-Sulphur Proteins,” Journal of Chromatography, (1979) pp. 351-356, vol. 172.
Robert C. Marshall, “Characterization of the Proteins of Human Hair and Nail by Electrophoresis,” The Journal of Investigation Dermatology, (1983) pp. 519-524, vol. 80.
W. G. Crewther, et al. “Helix-Rich Fraction from Low-Sulphur Proteins of Wool,” Nature, (Jul. 17, 1965) p. 295, No. 4994.
H. Lindley, et al., “Occurrence of the Cys-Cys Sequence in Keratins,” J. Mol. Biol., (1967) pp. 63-67, vol. 30.
Robert C. Marshall, “Genetic Variation in the Proteins of Human Nail,” The Journal of Investigate Dermatology, (1980) pp. 264-269, vol. 75.
M. E. Campbell, et al., “Compositional Studies of High-and Low-Crimp Wools,” Aust. J. Biol. Sci., (1972) pp. 977-1087, vol. 25.
P.J Reis, et al. “A Relationship between Sulphur Content of Wool and Wool Production by Merino Sheep,”0 Aust. J. Biol. Sci., (1967) pp. 153-163, vol. 20.
Robert C. Marshall, et al., “The Keratin Proteins of Wool, Horn and Hoof from Sheep,” Aust. J. Biol. Sci, (1977) pp. 389-400, vol. 30.
J.M. Gillespie. “Reaction of Sodium Borohydride with Wool,” nature, (Jan. 31, 1959) pp. 322-323, vol. 183.
David R. Goddard, et al., “A Study on Keratin,” J. Bio. Chem., (1934) pp. 605-614, vol. 106.
L.M. Dowlling, et al., “Isolation of Components from the Low-Sulphur Proteins of Wool By Fractional Preciptation Preparative Biochemistry,” (1974) pp. 203-226, vol. 4 (3).
W.G. Crewther, et al., “Reduction of S-Carboxymethylcysteine and Methionine with Sodium in Liquid Ammonia,” B
Keraplast Technologies Ltd.
Vinson & Elkins L.L.P.
Wax Robert A.
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