Studies on the high-sulphur proteins of reduced merino wool

Swart, L. S.; Parris, Deborah S.; Joubert, François J.

doi:10.1016/s0021-9673(73)30089-9

Cited by 9 publications

(7 citation statements)

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“…between the 50 kd Keratin Sequence and the Sequences of Other Keratins The amino acid composition and the molecular weight of the 50 kd epidermal keratin are similar to those of the microfibrillar keratins of hair and wool, but markedly different from those of the matrix keratins ( Table Table 1 Swart and Haylett, 1973;and Jones, 1975. ' Calculated from the predicted protein sequence in Figure 2.…”

Section: Homologiesmentioning

confidence: 93%

“…The complete sequences for several of the "high sulfur" matrix keratins of wool have been determined (for example, Swart and Haylett, 1973). A comparison of the sequence of the 50 kd epidermal keratin with these matrix keratin sequences revealed no significant homology between the two types of proteins.…”

Section: Homologiesmentioning

confidence: 99%

“…The matrix proteins, which are also called keratins, are mostly small proteins (6-20 kd). While the primary sequences of some of the matrix keratins have already been determined (for example, Swart and Haylett, 1973) only partial amino acid sequences of microfibrillar keratins have been obtained (Gough et al, 1978) and no sequence information is available for the cytoskeletal keratins. Thus the relationship of the cytoskeletal keratins to these other keratins has remained largely a matter of conjecture.…”

Section: Introductionmentioning

confidence: 99%

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The cDNA sequence of a human epidermal keratin: Divergence of sequence but conservation of structure among intermediate filament proteins

Hanukoglu

Fuchs

1982

Cell

293

206

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We have determined the DNA sequence of a cloned cDNA that is complementary to the mRNA for the 50 kilodalton (kd) human epidermal keratin. This provides the first amino acid sequence for a cytoskeletal keratin. Comparison of this sequence with those of other keratins reveals an evolutionary relationship between the cytoskeletal and the microfibrillar keratins, but shows no homology to matrix or feather keratins. The 50 kd keratin shares 28%-30% homology with partial sequences of other intermediate filament proteins, which suggests that keratins may be the most distantly related members of this class of fibrous proteins. Our computer analyses predict that the 50 kd keratin contains two long alpha-helical domains separated by a cluster of helix-inhibitory residues in the middle of the protein. These findings indicate that despite major sequence divergence among intermediate filament proteins, they retain sequences compatible with secondary structural features that appear to be common to all of them.

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Section: Homologiesmentioning

confidence: 93%

Section: Homologiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The cDNA sequence of a human epidermal keratin: Divergence of sequence but conservation of structure among intermediate filament proteins

Hanukoglu

Fuchs

1982

Cell

293

206

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“…The place of origin in the fibre and the composition of the polypeptides in the second group, with molecular weights between 32 000 and 25 000, are unknown. For merino wool, it has been shown that the polypeptides in the third group, with molecular weights between 18 000 and 8000, are high-sulphur and high-glycine/tyrosine polypeptides that originate in the protein matrix between the microfibrils [4,5]. Again, the same may be true of the polypeptides in this group from the other fibres.…”

Section: Referencesmentioning

confidence: 94%

Distinguishing between Different Animal Fibres by Electrophoresis of Polypeptides Dissolved from Them

Speakman

Horn

1987

Journal of the Textile Institute

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Samples of Lincoln wool, merino wool, mohair, cashmere, and alpaca were di88olved separately in alkaline reducing solutions. The resulting solutions were examined by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate.The technique separated up to seven classes of polypeptide with different molecular weights from each solution and was used to determine the polypeptide molecular weights.There are differences between the molecular weights of the polypeptides dissolved from different animal fibres, and in some cases the method can be used to distinguish between different animal fibres.Polypeptides were dissolved from 0.2-g samples of the five different animal fibres by treating the samples for 18 h at room temperature in 100 ml of a solution containing 0.2M mercaptoethanol and O.IM disodium hydrogen phosphate adjusted to pH 11.0. The cysteine residues in the polypeptides were not converted to S-carboxymethyl cysteine residues. The dissolved polypeptides were precipitated by acidifying the solutions, redissolved, and examined by polyacrylamide-gel electrophoresis (PAGE) in the presence of sodium dodecyl sulphate (SDS) on homogeneous 15% slab gels, Coomassie blue staining being used, as described previously [1]. This technique separates polypeptides with different molecular weights from the solutions of polypeptides and allows the molecular weights of the polypeptides to be determined.

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“…The extracts from wool contain three classes of protein (see Crewther, 1976): high-sulphur and high-tyrosine proteins derived from the matrix, and low-sulphur proteins from the microfibrils (Jones, 1976). The primary structures of 18 high-sulphur proteins (see Swart et al, 1976) and two high-tyrosine proteins (Dopheide, 1973;Marshall et al, 1980) are known.…”

Section: Introductionmentioning

confidence: 99%

The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments

Dowling¹,

Crewther²,

Inglis³

1986

Biochemical Journal

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Component 8c-1, one of four highly homologous component-8 subunit proteins present in the microfibrils of wool, was isolated as its S-carboxymethyl derivative and its amino acid sequence was determined. Large peptides were isolated after cleaving the protein chemically or enzymically and the sequence of each was determined with an automatic Sequenator. The peptides were ordered by sequence overlaps and, in some instances, by homology with known sequences from other component-8 subunits. The C-terminal residues were identified by three procedures. Full details of the various procedures used have been deposited as Supplementary Publication SUP 50133 (4 pp.) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1986) 233, 5. The result showed that the protein comprises 412 residues and has an Mr, including the N-terminal acetyl group, of 48,300. The sequence of residues 98-200 of component 8c-1 was found to correspond to the partial or complete sequences of four homologous type I helical segments previously isolated from helical fragments recovered from chymotryptic digests of microfibrillar proteins of wool [Crewther & Dowling (1971) Appl. Polym. Symp. 18, 1-20; Crewther, Gough, Inglis & McKern (1978) Text. Res. J. 48, 160-162; Gough, Inglis & Crewther (1978) Biochem. J. 173, 385]. Considered in relation to amino acid sequences of other intermediate-filament proteins, the sequence is in accord with the view that keratin filament proteins are of two types [Hanukoglu & Fuchs (1983) Cell (Cambridge, Mass.) 33, 915-924]. Filament proteins from non-keratinous tissues, such as desmin, vimentin, neurofilament proteins and the glial fibrillary acidic protein, which form monocomponent filaments, constitute a third type. It is suggested that as a whole the proteins from intermediate filaments be classed as filamentins, the three types at present identified forming subgroups of this class. The significant homologies between types I, II and III occur almost exclusively in segments of the chain that have been identified as having a coiled-coil structure together with the relatively short sections connecting these segments. The non-coiled-coil segments at the C- and N-termini show no significant homology between types, nor is homology in these segments apparent in all members of one type. Component 8c-1 does not show homology in its terminal segments with the known sequence of any other filamentin.(ABSTRACT TRUNCATED AT 400 WORDS)

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Studies on the high-sulphur proteins of reduced merino wool

Cited by 9 publications

References 0 publications

The cDNA sequence of a human epidermal keratin: Divergence of sequence but conservation of structure among intermediate filament proteins

The cDNA sequence of a human epidermal keratin: Divergence of sequence but conservation of structure among intermediate filament proteins

Distinguishing between Different Animal Fibres by Electrophoresis of Polypeptides Dissolved from Them

The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments

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