Studies on the High-Sulfur Proteins of Reduced Merino Wool

Haylett, Thomas; Swart, L. S.

doi:10.1177/004051756903901004

Cited by 41 publications

(10 citation statements)

References 29 publications

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“…Asquith was able to semi-quantitatively determine some peptide sequences in wool keratin by controlled hydrolysis of keratose fractions [37]. Similarly, partial hydrolysis was used to determine the amino acid sequence of wool proteins [38,39].…”

Section: Acid and Alkaline Treatmentmentioning

confidence: 99%

Keratinaceous Wastes and Their Valorization through Keratinolytic Microorganisms

Ningthoujam¹,

Tamreihao²,

SaikatMukherjee³

et al. 2018

Keratin

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Keratin is a fibrous protein mainly found in higher vertebrates such as mammals, birds, and reptiles. It is also a major constituent of human epithelial tissues. Major keratinaceous wastes include skin, hair, wool, feather, horns, hooves, and nails. Large amounts of such wastes are generated from meat industry, poultry houses, and wool industry etc. Though keratinous wastes contain about 90% protein, keratin is usually recalcitrant to normal proteases. Such wastes have been traditionally digested using physico-chemical methods. But such techniques are energy-intensive and technologically demanding. Also, such approaches lead to degradation of certain amino acids such as lysine. In nature, keratinaceous wastes don't accumulate indicating that keratinolytic microorganisms exist in nature. Keratinase producing strains are distributed among bacteria, fungi, and actinobacteria etc. Hence, potent keratinolytic microbes and their enzymes may be used for valorization of keratinous wastes. Efficient degradation of such wastes may generate value-added products such as feed additives, agricultural biofertilizers, and cosmetics. This chapter will give a comprehensive overview of types of keratinaceous wastes, kinds of keratinolytic microbes and keratinases, and valorization of such wastes using keratinase producing strains and/or keratinases.

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Section: Acid and Alkaline Treatmentmentioning

confidence: 99%

Keratinaceous Wastes and Their Valorization through Keratinolytic Microorganisms

Ningthoujam¹,

Tamreihao²,

SaikatMukherjee³

et al. 2018

Keratin

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“…10). As for wool protein IIIB2 (Haylett & Swart, 1969), protein M1.2 was not cleaved after the lysine residue in position 23, and was only partially cleaved after the arginine residue in the penultimate position.…”

Section: Discussionmentioning

confidence: 91%

“…Partial acid hydrolysis. Partial cleavage of the peptide bonds of peptide TlQl was achieved by the method of Haylett & Swart (1969). The peptide (1j1umol) was incubated with 1 ml of IOM-HCl at 40C for 18 h and the solution was freeze-dried.…”

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confidence: 99%

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Studies on the high-sulphur proteins of reduced mohair. The isolation and amino acid sequence of protein scmkb-m1.2

Parris

Swart

1975

Biochemical Journal

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The complete amino acid sequence of mohair protein, SCMKB-M1.2 (97 residues), was determined. The protein was isolated from reduced and carboxymethylated mohair by chromatography on DEAE-cellulose phosphate. Peptides for sequence determination were obtained by digestion with trypsin, pepsin, chymotrypsin, thermolysin and papain, and were fractionated by DEAE-cellulose chromatography, paper chromatography and electrophoresis. The sequence of the peptides were determined by the Edman degradation method (by use of both the Beckman Sequence and a non-automatic procedure), and by partial acid hydrolysis. The protein is closely homologous to wool protein SCMKB-IIIB2, and also contains acetylated alanine as N-terminal amino acid.

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“…They have led to the recognition of two major protein fractions, the highand low-sulphur protein fractions, and another fraction of varying importance from wool type to wool type that is characterized by being rich in glycine and tyrosine residues. The complete sequences of seven proteins of the high-sulphur type and one sequence of a high-glycine-tyrosine protein have been published (Haylett & Swart, 1969;Haylett et al, 1971; 1972a,b; Elleman & Dopheide, 1972;Dopheide, 1973;Swart, 1973). Considerable progress has also been made in sequencing low-sulphur-protein fractions from wool (W. G. Crewther, personal communication) and in a related field the sequence of a protein from emu feather has been reported (O'Donnell, 1973).…”

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confidence: 99%

The reactivity of the disulphide bonds of wool

Lindley

Cranston

1974

Biochemical Journal

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1. Fully reduced and S-carboxymethylated wool samples were prepared in which either the readily reducible cystine bonds or those that could only be reduced with difficulty were specifically labelled with iodo[2-(14)C]acetate; these two cystine fractions correspond to the (A+B) and (C+D) cystine fractions respectively, of Middlebrook & Phillips (1942). 2. Radioactively labelled peptides were isolated from partial acid hydrolysates of these wool samples. 3. It appears that the (A+B) cystine residues probably owe their increased reactivity to being in a more polar environment. 4. The implication of these results for the problem of characterizing the disulphide bonds of wool is briefly discussed.

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Studies on the High-Sulfur Proteins of Reduced Merino Wool

Cited by 41 publications

References 29 publications

Keratinaceous Wastes and Their Valorization through Keratinolytic Microorganisms

Keratinaceous Wastes and Their Valorization through Keratinolytic Microorganisms

Studies on the high-sulphur proteins of reduced mohair. The isolation and amino acid sequence of protein scmkb-m1.2

The reactivity of the disulphide bonds of wool

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