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Tuesday, May 5, 2020 | History

2 edition of interaction of amino acid residues in wool keratin with reactive dyes. found in the catalog.

interaction of amino acid residues in wool keratin with reactive dyes.

David Kui-Tak Chan

interaction of amino acid residues in wool keratin with reactive dyes.

by David Kui-Tak Chan

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Published in Bradford .
Written in English


Edition Notes

Ph.D. thesis. Typescript.

SeriesTheses
The Physical Object
Pagination250p.
Number of Pages250
ID Numbers
Open LibraryOL13652986M

CORFIELD MC, ROBSON A. The amino acid composition of salmine. Biochem J. Oct; 55 (3)– [PMC free article] Cuthbertson WR, Phillips H. The action of alkalis on wool: 1. The subdivision of the combined cystine into two fractions differing in their rate and mode of reaction with alkalis. Biochem J. ; 39 (1):7–Cited by:   In textile industry, the keratin hydrolyzate modified with a cationic agent was an alternative to sodium sulfate for enhancing the uptake of reactive dyes by cotton fabrics ; the superheated water hydrolyzed keratin was employed as a foaming agent in the foam dyeing of cotton and wool fabrics ; the keratin extracted by the reduction method Cited by: 5.

KERATIN AMINO ACIDS ingredient for cosmetics formulations – find latest products launched and their applications in relevant industry news and technical articles. Abstract. 1. The amino acid sequence of protein SCMK-B2A, a reduced and S-carboxymethylated protein from the high-sulphur fraction of wool, has been determined This protein of amino acid residues displays both a high degree of internal homology and extensive external homology with other members of the SCMK-B2 group of by:

Fluorescence spectroscopy and molecular dynamics (MD) simulation are combined to characterize the interaction of two organic fluorescent dyes, rhodamine 6G (R6G) and an oxazine derivative (MR), with the amino acid tryptophan in aqueous solution. Steady-state and time-resolved fluorescence quenching experiments reveal the formation of essentially nonfluorescent ground-state dye/Trp Cited by: Abstract. We present the complete nucleotide and deduced amino acid sequences of a mouse epidermal keratin subunit of 60, Da. The keratin possesses a central alpha-helical domain of four tracts (termed 1A, 1B, 2A, and 2B) that can form coiled-coils, interspersed by short linker sequences, and has non-alpha-helical terminal by:


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Interaction of amino acid residues in wool keratin with reactive dyes by David Kui-Tak Chan Download PDF EPUB FB2

The Dyeing of Wool with Reactive Dyes. reactivity of an acrylamido dye towards wool, silk, and nylon. Amino–acid analyses of wool dyed to heavy depths with unmetallised and 1: 2 metal. Commercial Reactive Dyes for Wool The Chemistry of Reactive Dyes Nucleophilic Substitution Reactions Michael Addition Reaction Specific Reactive Dyes for Wool Application Procedures Auxiliary Agents Dyeing Processes Used with Reactive Dyes Effect of Reactive Dyes on.

The reactivity of keratin from wool models the reactivity of keratin from low-value sources such as cattle hair. Introduction. Wool with up to 95% keratin by weight is a rich and pure source of intermediate filament proteins (IFPs) which can be Cited by: The reactions of wool with sulfamic acid have been investigated and the results show that under the conditions used, the reactions are similar to those of sulfuric acid and wool.

The majority of reaction takes place on alcoholic amino acids, but some reaction does take place on primary amino groups.

No reaction takes place on the cystine linkage. The binding of three acid dyes of slightly differing composition to a soluble wool keratin derivative has been measured by the dialysis-equilibrium method.

The data satisfy the Klotz-Scatchard equation for the binding of small ions to proteins but the maximum amount of dye bound is much less than that equivalent to the number of basic side chains on the protein, given by amino acid : B.S Harrap.

Abstract. The molecules of which natural fibres are composed abound in reactive groups. Cellulosic fibres are polymers consisting of chains of D-glucose units each containing three hydroxyl groups, and protein fibres are built from a variety of amino acid residues.

sheep,M the sheep's diet,' and even the time of the year.6 The nature of the amino acid side chains and the percentages of the individual amino acids present in the keratin are very important to the dyeing process, as acidic and basic side chains provide sites with which to bind Size: 2MB.

On the basis of amino acid analysis conclusions were drawn on the photodegradation mechanism of wool, both uncoloured and dyed with reactive dyes.

Reactive dyes protect wool against. The various enzymes or enzyme systems that have been demonstrated in wool roots include alkaline and acid phosphatases, pyrophosphatase or adenosine diphosphatase or botb, a system converting metaphosphate to orthophosphate, thymonucleic acid depolymerase, phosphorylase, a dehydrogenase (with an unidentified natural substrate) acting on some L-amino acids and glycine, catalase, and a system catalyzing the absorption FORMATION, COMPOSITION, AND PROPERTIES OF KERATINS of carbon by: A) formation of the maximum number of hydrophilic interactions.

B) maximization of ionic interactions. C) minimization of entropy by the formation of a water solvent shell around the protein. D) placement of hydrophobic amino acid residues within the interior of the protein.

E) placement of polar amino acid residues around the exterior of the. Amino acid residues such as aspartic acid, glutamic acid, cysteine and histidine will form strong complexes with Cr(III). A major advance in reactive dyes for wool occurred in with the launch of the Lanasol dyes Representation of bound cystine/cysteine in wool by: 4.

The carboxylic acid and amino groups in the keratin molecule confer affinity for basic and acid dyes. Acid dyes are extensively used for dyeing wool fabrics.

Since the bonds between dye anions and amino groups in the wool fibre are easily broken and re- formed, dyes. Reis, P. J.,Effects of amino acids on the growth and properties of wool, in: Physiological and Environmental Limitations to Wool Growth (J.

Black and P. Reis, eds.), University of New England Publications Unit, New South Wales, pp. – Google ScholarCited by: Treatment of wool fabric for short periods at 3° and 21° with concentrated sulfuric acid confers on the fabric a marked resist to some acid dyes. By controlling the sulfation conditions, the accompanying loss in strength is minimized.

This resist is stable to prolonged boiling in the dyebath and to acid and alkali. -keratin contains a 7 residue pseudorepeat (a-b-c-d-e-f-g) within the central ~ segment of the molecule Residues at position a and d are hydrophobic and are responsible for the association of the two subunits The Å spacing of the -helices optimize the association of the hydrophobic residuesFile Size: KB.

Effective Method Development on Wool Dyeing by Using Fl Based Cotton-reactive Dyes January International Journal of Scientific and Engineering Research 6(6) amino acid based compounds particularly for cationization of jute ultimately aiming at dyeability with reactive dyes.

Hence, it is thought that this type of cationic modification of jute may improve dyeability with anionic (reactive) dyes. Such studies for jute textiles have not been reported so Size: KB. Wool is chemically a polypeptide polymer made up of 18 amino acids with α- keratin arranged in helical structure.

Apart from long helical structure, the wool polymer chain also has free thiol groups, amino acid residue with amide group and protonated carboxyl acid group side chains (Church et al ). G C A T genes T A C G G C A T Review Wool Keratin-Associated Protein Genes in Sheep—A Review Hua Gong 1,2, Huitong Zhou 1,2, Rachel H.

Forrest 3, Shaobin Li 1, Jiqing Wang 1, Jolon M. Dyer 4, Yuzhu Luo 1,* and Jon G. Hickford 1,2,* 1 International Wool Research Institute, Faculty of Animal Science and Technology, Gansu Agricultural University, LanzhouChina. In general, a single keratin protein polymer chain consists of a polypeptide backbone formed from the condensation of L-amino acids, which have side chains from the 22 common amino acids.

The most abundant side chains include the salt-forming aspartic and glutamic acid residues, the basic lysine and arginine residues as well as the sulfur-rich.

Fig. 3 – Effect of treatment of wool with keratin/ECH (4 % w/w) on its dyeability with C.I. Acid Blue (2 & 4% owf, MLR 5 at 85° C)pH Fig.

1 – Effect of treatment of wool fabrics with keratin/ECH on its dyeability with both acid and reactive dyes (4 % owf, pH 5, MLR60 min)Cited by: 3.The B-4 chain consisted of 96 amino acid residues and had a mol. wt. of 10, in the S-carboxymethylated form. The N-terminus of this protein was an N-acetylserine residue.

The B-4 protein contained 7 S-carboxymethylcysteine residues, 6 of which were located in the N-terminal region (residues ), and the other one in the by: The above analyses are approximations and are governed by the acid dissociation constants of the –NH3 + 3 and –COOH residues, conveniently expressed as pK a values; for example at 25 °C lysine ε-amino has a pK a value of about and the glutamic acid terminal carboxylate is about Possibly of even greater significance, in terms of positive charge contribution, is the guanidyl side Cited by: 2.