A series of events occurred when wool was heated in vacuum. At some stages structural changes in the thermally-treated wool were observed, as reflected in the low-angle x-ray diffraction patterns. An increase in the intensity of the 39 Å meridional reflection and the appearance of a 4-point diagram with azimuthal angle of 45° at about 46 Å spacing were observed when wool was heated near 170°C for 90 min. Similar results were found in samples heated at higher temperatures but for shorter time. The most heat-resistant meridional reflection is the 66 Å.
The low-angle x-ray diffraction patterns of plasma-treated wool showed only disappearance of the sharp lipid ring at 48 Å. No intensification of any reflection was observed. Prolonged treatment with plasma destroys the low-angle x-ray diffraction pattern of wool.
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References
1.
AlterH.KivimagiK., The Melting of Keratin, Textile Res. J.39, 608–610 (1969).
2.
AsquithR. S.OtterburnM. S., Basic Amino Acids in Heated Keratin, J. Textile Inst.60, 208–210 (1969).
3.
AsquithR. S.OtterburnM. S., Self-Crosslinking in Keratin Under the Influence of Dry Heat, Appl. Polym. Symp. No. 18, 277–287 (1971).
4.
BenditE. G., Melting of α-Keratin in Vacuo, Textile Res. J.36, 580–581 (1966).
5.
BonartR.SpeiM., Grundlagen fur die Interpretation der Rontgenkleinwinkeldiagramme von α-Keratin, Kolloid-Z. Z. Polym.250, 385–393 (1972).
6.
CoreyR. B.WyckoffR. W. G., Long Spacings in Macromolecular Solids, J. Biol. Chem.114, 407–416 (1936).[.
7.
CrightonJ. S.HappeyF., Differential Thermal Analysis of Keratin and Related Protein Fibers, in “Symposium on Fibrous Proteins,” Australia, 1967, Ed. by CrewtherW. G., Plenum Press, New York, 1968, pp. 409–420.
8.
DobbM. G.FraserR. D. B.MacRaeT. P., “The Structure of the Keratin Filament,” 3e Congres International de la Recherche Textile Lainiere, Paris (CIRTEL) I, 95–102 (1965).
9.
FoxS. W.HaradaK.RohlfingD. L., The Thermal Copolymerization of α-Amino Acids, paper 5 in “Polyamino Acids, Polypeptides, and Proteins,” Ed. by StahmannM. A., Univ. Wisconsin Press, Madison, Wis., 1962, pp. 47–54.
10.
FraserR. D. B.MacRaeT. P., Evidence of Regularities in the Chemical Structure of α-Keratins, Nature179, 732–733 (1957).
11.
FraserR. D. B.MacRaeT. P.RogersG. E., Recent Observations on the Structure of α-Keratin, J. Textile Inst. Trans.51, 497–505 (1960).
12.
HalyA. R.FeughelmanM., The X-Ray Diffraction Pattern of Iodinated Wools, Textile Res. J.30, 622–623 (1960).
13.
HalyA. R.SnaithJ. W., Differential Thermal Analysis of Wool—The Phase-Transition Endotherm Under Various Conditions, Textile Res. J.37, 898–907 (1967).
14.
HeidemannG., Project No. UR-E10-(20)-8, Grant No. FG-Ge-103, Report No. 3, 1966, German Wool Research Institute, Aachen, W. Germany.
15.
HeidemannG.HalbothH., X-Ray Evidence of Regularly Distributed Lysine in α-Keratin, Nature213, 71–72 (1967).
16.
HorioM.KondoT.SekimotoK.FunatsuM., Pyrolysis of Wool in Sealed Tubes, 3e Congres International de la Recherche Textile Lainiere, Paris (CIRTEL) II, 182–200 (1965).
17.
HowittF. O., The Yellowing of Wool: A Survey of the Literature, J. Textile Inst. Trans.55, 136–145 (1964).
18.
JanowskiZ.SpeakmanJ. B., The Action of Heat on Wool, 3e Congres International de la Recherche Textile Lainiere, Paris (CIRTEL) II, 157–165 (1965).
19.
KassenbeckP.StayA., Denaturierung keratinischer Proteine unter Einwirkung von Hitze, Progr. Colloid & Polym. Sci.57, 123–132 (1975).
20.
KratkyO.SekoraA.ZahnH.FritzeE. R., Kleinwinkel-Rontgen-interferenzen bei nitrierten Faserkeratinen, Z. Naturforsch.10b, 68–72 (1955).
21.
KulkarniV. G., The Separation of Cortical Cells and the Pyrolysis of Wool Keratin, Textile Res. J.45, 89–90 (1975).
22.
LeeK. S.PavlathA. E.MenefeeE., “Single Fiber Studies on Plasma Treated Wool,” 167th National ACS Meeting, Los Angeles, CA, April, 1974: abstract, CELL:59.
23.
LeeK. S.PavlathA. E., “The Effect of Gas Composition on Wool in an Electric Glow Discharge,” Proc. Int. Wool Textile Res. Conf., Aachen, 1975, in Schriftenreihe Deutsches Wollforschungsinstitut an der Technischen Hochschule Aachen, 1976.
24.
MechamD. K.OlcottH. S., Effect of Dry Heat on Proteins, Ind. Eng. Chem.39, 1023–1027 (1947).
MillardM. M.WindleJ. J.PavlathA. E., Plasma Synthesis of Fluorocarbon Films, J. Appl. Polym. Sci.17, 2501–2507 (1973).
27.
MilliganB.HoltL. A.CaldwellJ. B., The Enzymic Hydrolysis of Wool for Amino Acid Analysis, Appl. Polym. Symp. No. 18, 113–125 (1971).
28.
PandeA., Differential Thermal Analysis and its Application, Lab. Practice14, 1048–1051 (1965).
29.
RichardsH. R.SpeakmanJ. B., The Iodination of Wool, J. Soc. Dyers Col.71, 537–544 (1955).
30.
RusznakI.TrezlL.BereckA.BidloG., Influence of Short Thermal Treatments on Wool, Appl. Polym. Symp. No. 18, 175–183 (1971).
31.
SimpsonW. S.WoodsH. J., Enhancement of the High-Spacing Meridional Reflexions in the X-Ray Photograph of Keratin Impregnated with Heavy-Metal Salts, Nature185, 157 (1960).
32.
SpeiM.HeidemannG.HalbothH., Further X-Ray Evidence of Regularly Distributed Lysine in α-Keratin, Nature217, 247 (1968).
33.
SpeiM.HeidemannG.ZahnH., X-Ray Evidence of the “198 Å Period” in α-Keratin, Naturwiss.55, 346 (1968).
34.
SpeiM., Rontgenkleinwinkeluntersuchungen an Carboxylgruppenmarkiertem α-Keratin, Kolloid-Z. Z. Polym.238, 436–438 (1970).
35.
SpeiM., The Influence of Detergents on Low-Angle X-Ray Diffraction Patterns of α-Keratin, Appl. Polym. Symp. No. 18, 659–662 (1971).
36.
SpeiM., Rontgenographische Nachweise der fundamentalen 198 Å Periodizitat in α-Keratin, Kolloid-Z. Z. Polym.250, 207–213 (1972).
37.
SpeiM., Rontgenkleinwinkeluntersuchungen zur Frage einer geordneten Matrix in α-Keratin, Kolloid-Z. Z. Polym.250, 214–221 (1972).
38.
SpeiM., Structure of α-Keratin, Textile Res. J.43, 692–693 (1973).
39.
WilsonG. A., Low-Angle X-Ray Diffraction Studies of Reduced and Silver-Stained α-Keratin, Polymer13, 63–68 (1972).
40.
WeclawowiczM.ReitzerM.-Th.SchutzR. A., Evolution des Caracteristiques et des Proprietes Chimiques de Fibres Proteiniques Naturelles de Structures Differenciees sous L'Effet de Traitements a Haute Temperature, 3e Congres International de la Recherche Textile Lainiere, Paris (CIRTEL) II, 179–185 (1965).
41.
ZahnH.KohlerK., (The Action of Nitric Acid on Albuminoids. I. New Roentgen Interference Action of Nitrated Fibroin and Keratin), Z. Naturforsch.5b, 137–138 (1950).
