Reactions of phosphine sulphides with aryl-lithiums

Corfield, J. R.; Trippett, S.

doi:10.1039/j39710000334

Cited by 4 publications

(4 citation statements)

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“…(ii) The N-terminal sequence of peptide CNBr-1 (residues 60-89) prepared from a mixture ofcomponent-8 subunits (Thompson & O'Donnell, 1967). This sequence confirmed the positioning of peptide Ch-2, as also did data of Corfield & Fletcher (1969), which corresponded to residues 57-76.…”

Section: Supplementary Informationsupporting

confidence: 64%

“…Sequences of a total of 21 tryptic and chymotryptic peptides isolated in an early study on a fraction US3 from oxidized wool proteins (Corfield et al, 1967;Corfield & Fletcher, 1969) can be matched with sequences in component 8c-1 totalling 70 residues. Other peptides from fraction US3 were homologous with sequences in component 8c-1.…”

Section: General Aspects Of the Analysismentioning

confidence: 99%

“…The low-sulphur proteins, which range in Mr from 45000 to 58000 (Woods, 1979), comprise two families, each consisting offour homologous subunits: components 5, 7a, 7b and 7c, and components 8a, 8b, 8c-1 and 8c-2 (Crewther et al, 1980a). Earlier attempts to obtain amino acid sequence data from a fraction containing low-sulphur proteins (Corfield et al, 1967;Corfield & Fletcher, 1969) and from a fraction enriched in component 8 (Thompson & O'Donnell, 1967;Hosken et al, 1968;O'Donnell, 1969) provided some short segments of sequence and demonstrated heterogeneity in the preparations used. Complete amino acid sequences have been determined for Abbreviation used: h.v.p.e., high-voltage paper electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Supplementary Informationsupporting

confidence: 64%

Section: General Aspects Of the Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…Most phosphetane derivatives are stable toward organolithium nucleophiles, but a few examples of additions of organolithium derivatives to phosphetanium salts, sulfides, and oxides have been reported. These additions provoke ring openings 30 and, in certain cases, migration of a phenyl substituent from phosphorus to the γ-carbon atom, 96,[100][101][102] as shown in eqs 25 and 26.…”

Section: Ring-opening Reactionsmentioning

confidence: 99%