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  • 1
    Electronic Resource
    Electronic Resource
    A study of the interaction of sodium dodecyl sulphate with the proteins of human heel stratum corneum (1987)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of cosmetic science 9 (1987), S. 0 
    Details
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The aim of this research is to study the in vitro interaction of the anionic surfactant sodium dodecyl sulphate with human heel callus with special regard to the callus proteins.The sorption of SDS by callus is analysed at different pH values, demonstrating the expected maximum binding of the anionic surfactant at low pH. In both surfactant and blank solutions, swelling of the callus pieces occurs but to different extents. The sorption of SDS by callus is accompanied by a loss of free amino acids and proteins. The protein composition of the callus residues after chemical treatment and of the corresponding treatment baths is examined by amino acid analysis and shows differences in the respective molar amino acid ratios. Results obtained with more specific techniques, such as gel electrophoresis and immunoblotting, demonstrate identical as well as different protein components in the treatment baths depending on the experimental conditions (pH, blank or SDS). Although effects due to the surfactant treatment are in principle more distinct than with blank experiments, those of the latter cannot be neglected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1467-2494.1987.tb00458.x
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  • 2
    Electronic Resource
    Electronic Resource
    Contributions to the chemistry of human hair: III. Protein chemical aspects of permanent waving treatments (1989)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of cosmetic science 11 (1989), S. 0 
    Details
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The influence of permanent waving on hair proteins was studied in order to obtain additional information about the chemistry of this cosmetic treatment. It was shown by amino acid analysis that with increasing reduction time during treatment fewer disulphide bonds were reformed in hair during subsequent reoxidation. Simultaneously, an increasing amount of sulphur-containing material is liberated from the hair, as demonstrated by the sulphur balance calculated from the sulphur-containing amino acids. The amount liberated is increased when an extensive soaking of the samples in water between the reduction and reoxidation step is performed. Comparing treatments with the use of reducing solutions of pH values between 7.5 and 10.0, it was found that the largest amount of cystine cleavage occurs at pH 9.0. All hair samples reduced at pH values above pH 8.5 showed incomplete reformation of the disulphide bonds during subsequent reoxidation. This was indicated by the content of free SH-groups and cysteic acid, as quantified by amino acid analysis. The damage to the hair proteins due to permanent waving was further confirmed by the determination of the pronase solubility. The reductive treatment of hair at pH 7.5 led to a relatively low degree of reduction, however all sulphur bonds were reformed during subsequent reoxidation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1467-2494.1989.tb00511.x
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  • 3
    Electronic Resource
    Electronic Resource
    Contributions to the chemistry of human hair. 1. Analyses of cystine, cysteine and cystine oxides in untreated human hair (1987)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of cosmetic science 9 (1987), S. 0 
    Details
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amino acid analysis, photometry and polarography were selected as analytical methods for the determination of thiol and disulphide groups in untreated human hair and the results are discussed. The pre-treatments necessary for the different analytical methods, e.g., hydrolysis, to some extent already induce chemical changes of the cysteine and cystine derivatives leading to method-dependent differences in the results. In many cases the partial oxidation products of cystine are supposed to be responsible for this effect. Electron Spectroscopy for Chemical Analysis (ESCA), as an analytical method for the determination of the cystine oxides, was found to be inapplicable due to insufficient resolution and sensitivity, whereas by the use of Fourier Transform Infrared (FTIR) Spectroscopy the sulphur-oxygen vibrations could be analysed and cystine monoxide and cystine dioxide were detected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1467-2494.1987.tb00467.x
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  • 4
    Electronic Resource
    Electronic Resource
    Wool as a Biological Composite Structure (1980)
    s.l. : American Chemical Society
    Industrial and engineering chemistry 19 (1980), S. 496-501 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/i360076a005
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  • 5
    Electronic Resource
    Electronic Resource
    Chemische Synthese von Proteinen (1967)
    Springer
    Naturwissenschaften 54 (1967), S. 396-402 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00603134
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  • 6
    Electronic Resource
    Electronic Resource
    Zum Reaktionsmechanismus von Glutaraldehyd mit Proteinen (1981)
    Springer
    Monatshefte für Chemie 112 (1981), S. 1313-1323 
    Details
    ISSN: 1434-4475
    Keywords: Crosslinking mechanism ; N-Alkyl-1,4-dihydropyridines ; N,N′-Alkyl-1,5-diiminopentanes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interaction of glutaraldehyde with model aliphatic amines was studied in order to understand the crosslinking reaction of glutaraldehyde with proteins. The reaction in organic solvents gave N-alkyl-1,4-dihydropyridines and N,N′-dialkyl-1,5-diiminopentanes. The isolated products are new or were previously described by us for the first time1. Hydration of the reaction products led to stable N-alkylpiperidines and N,N′-dialkyl-1,5-diaminopentanes. In aqueous solution the reaction depends on thepH: at apH above 7, N-alkyl-1,4-dihydropyridines and at apH below 7, polymers were obtained. For the crosslinking reaction of proteins with glutaraldehyde the following mechanism is proposed: Monomeric glutaraldehyde reacts with the protein to give intermediate N-alkyl-2,6-dihydroxypiperidines. Intramolecular dehydration leads to the corresponding N-alkyl-1,4-dihydropyridines. Condensation of the cyclic monohydrate of glutaraldehyde and N-alkyl-2,6-dihydroxypiperidines gives linear polymeric crosslinks containing α-oxo-N-alkylpiperidine units.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00904683
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  • 7
    Electronic Resource
    Electronic Resource
    Reaktion von reduzierter A- und B-Kette mit Insulin [15] (1968)
    Springer
    Diabetologia 4 (1968), S. 118-122 
    Details
    ISSN: 1432-0428
    Keywords: Beef insulin ; reduced insulin-A-chain ; partially oxidized insulin-A-chain ; reduced insulin-B-chain ; A-chain oligomers ; B-chain polymers ; thiol-disulphide interchange ; thiol groups ; reduction ; stability ; inactivation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé Quand l'insuline réagit avec la chaîne B bithiol (préparée à partir de l'insuline de boeuf) dans un rapport molaire 1∶1, à pH 9.5, en présence ou en l'absence d'oxygène de l'air, il se forme des chaînes oligomères et polymères reliées par des liaisons disulfure. — Des quantités équimolaires de chaîne-A d'insuline, sous sa forme tetrathiol, provoquent également une transformation partielle de l'insuline en produits oligomères et polymères, quand elles sont mises en réaction avec l'insuline à pH 9.3, en présence d'oxygène de l'air. Cependant, la chaîne A partiellement oxydée, contenant en moyenne 2 moles de groupement SH par mole de chaîne A, n'attaque pas l'insuline dans ces conditions de réaction.
    Abstract: Zusammenfassung Aus Rinderinsulin isolierte B-Kette in der Bisthiolform reagiert mit Insulin bei der Umsetzung im Molverhältnis 1∶1 und pH 9.5 sowohl in Gegenwart als auch bei Ausschluß von Luftsauerstoff unter Bildung von oligomeren und polymeren über Disulfidbindungen verbundenen Ketten. — Auch Insulin-A-Kette in der Tetrathiolform wandelt Insulin bei pH 9.3 in Gegenwart von Luftsauerstoff teilweise in oligomere und polymere Produkte um, wenn äquimolare Mengen in die Reaktion eingesetzt werden. Unter gleichen Reaktionsbedingungen greift partiell oxydierte A-Kette, die durchschnittlich 2 Mole SH-Gruppen pro Mol Kette enthält, Insulin nicht an.
    Notes: Summary When insulin is reacted with bis-thiol-B-chain (prepared from beef insulin) in a molar ratio 1∶1 at pH 9.5 in the presence or absence of air, oligomeric and polymeric chains, linked by disulfide bonds, are formed. Equimolar amounts of insulin-A-chain in its tetrathiol form when brought into reaction with insulin at pH 9.3 in the presence of air also cause a partial transformation of insulin into oligomeric and polymeric products. Partially oxidized A-chain, however, containing an average of 2 moles SH-groups per mole of A-chain, does not attack insulin under these reaction conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01219431
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  • 8
    Electronic Resource
    Electronic Resource
    Zum Vorkommen von Isopeptidbindungen in erhitztem Milcheiweiß (1976)
    Springer
    European food research and technology 160 (1976), S. 377-381 
    Details
    ISSN: 1438-2385
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Description / Table of Contents: Zusammenfassung Milch, Milcherzeugnisse und einzelne Milchproteine wurden in unterschiedlichem Ausmaß trocken oder als wässriges System erhitzt. Die Proben wurden nach vollstdndiger Hydrolyse der Peptidbindungen (α-Amidbindungen) durch ein System von vier Proteinasen bzw. Peptidasen auf das Vorkommen von Isopeptiden untersucht. Dafür wurden zwei Ionenaustauschsysteme entwickelt, die eine Trennung von N ɛ -(β-Asparagyl-)lysin ( ) sowie N ɛ -(γ-Glutamyl-)lysin ( ) von Aminosäuren ermoglicht. In 24 Std trocken auf mindestens 120° C erhitztem Milcheiweiß waren 2–5% des Lysins in -Bindungen überführt. Unter den Erhitzungsbedingungen der milchwirtschaftlichen Praxis entstehen keine Isopeptidbindungen.
    Notes: Summary Milk, milk products and individual milk proteins were subjected to different heat treatments either as powders or in aquous systems. After complete hydrolysis of the peptide bonds (α-amide bonds) by a system of four proteinases or peptidases, respectively, the samples were analysed for isopeptides. For this purpose, two chromatographic ion exchange systems were developed, each of which separates N ɛ -(β-aspartyl-)lysine ( ) as well as N ɛ -(γ-glutamyl-)lysine ( ) from the common amino acids. In samples, heated 24 h for at least 120° C, 2–5% of the lysine residues are incorporated in -bonds. Under the heating conditions used in dairy practice, no isopeptide bonds were formed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01106328
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  • 9
    Electronic Resource
    Electronic Resource
    Untersuchungen an Kollagen (1962)
    Springer
    Colloid & polymer science 180 (1962), S. 26-35 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Zusammenfassung 1. Eine aus Rindersehnenkollagen gewonnene Folie wurde mit l,5-Difluor-2,4-dinitrobenzol (FFDNB) umgesetzt. Die Präparate wurden gerbereichemisch untersucht und der Anstieg der Schrumpfungstemperatur und die Abnahme der Trypsinlöslichkeit durch eine bifunktionelle Reaktion zwischen FFDNB und den Aminogruppen des eingebauten Lysins und Hydroxylysins erklärt. 2. Die fünf bei einer Umsetzung des bifunktionellen FFDNB mit denɛ-Aminogruppen des Lysins und Hydroxylysins möglichen Verbindungen wurden zum Teil erstmalig synthetisiert und im Totalhydrolysat von DNP-en-Kollagen nach Chromatographie an Nylon-66-Pulversäulen isoliert und identifiziert. 3. Die Isolierung von DNP-en-Bis-lysin und -Bishydroxylysin in Substanz gelang aus dem Hydrolysat von 15 g DNP-en-Kollagen.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01499480
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  • 10
    Electronic Resource
    Electronic Resource
    Synthese von radioaktivem 1-Fluor-2,4-dinitrobenzol und Anwendung zur Bestimmung der Cysteingruppen in Wollkeratin (1961)
    Springer
    Colloid & polymer science 179 (1961), S. 49-60 
    Details
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Zusammenfassung Aus 360,6 mg Anilinhydrochlorid-C-14 (im Benzolring markiert) wurden über vier Stufen 322,1 mg 1-Fluor-2,4-dinitrobenzol (FDNB) spezifische Radioaktivität 1,15 mC/mMol) mit einer Ausbeute von 62,2% der Theorie synthetisiert. Es wurde eine Mikromethode zur quantitativen. Bestimmung von SH-Gruppen in Wolle mit radioaktivem FDNB ausgearbeitet, die es gestattet, den SH-Gehalt in 50–100γ Wolle zu ermitteln. Die Abhängigkeit der Dinitrophenylierung der SH-Gruppen von der Konzentration an FDNB, dem pH-Wert der Flotte, der Reaktionstemperatur und der Reaktionsdauer wurde untersucht. Eine spezifische Dinitrophenylierung der SH-Gruppen lie\ sich auch bei niedrigen pH-Werten der Flotte nicht erreichen. Es erfolgte immer eine beträchtliche, wenn auch langsamere Dinitrophenylierung anderer reaktionsfähiger Gruppen der Wolle, und die Dinitrophenylierung der SH-Gruppen war bei niedrigen pH-Werten nicht quantitativ. Im bicarbonatalkalischen Medium lie\ sich eine Dinitrophenylierung der alkoholischen OH-Gruppen des Serins nachweisen. Unter optimalen Bedingungen wurde ein Cysteingehalt des untersuchten Kammzugs von 22,2Μ Molen/g Wolle festgestellt.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01520593
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