The amino acid sequence of protein SCMK-B2A from the high-sulphur fraction of wool keratin.
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ABSTRACT:
SUBMITTER: Elleman TC
PROVIDER: S-EPMC1174523 | biostudies-other | 1972 Dec
REPOSITORIES: biostudies-other
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Project description:1. The amino acid sequence of a protein from the reduced and carboxymethylated high-sulphur fraction of wool has been determined. 2. The sequence of this S-carboxymethylkerateine (SCMK-B2C) of 151 amino acid residues displays much internal homology and an unusual residue distribution. Thus a ten-residue sequence occurs four times near the N-terminus and five times near the C-terminus with few changes. These regions contain much of the molecule's half-cystine, whereas between them there is a region of 19 residues that are mainly small and devoid of cystine and proline. 3. Certain models of the wool fibre based on its mechanical and physical properties propose a matrix of small compact globular units linked together to form beaded chains. The unusual distribution of the component residues of protein SCMK-B2C suggests structures in the wool-fibre matrix compatible with certain features of the proposed models.
| S-EPMC1174011 | biostudies-other
Project description:The complete amino acid sequences of wool protein SCMKB-IIIA3 (131 residues) and a minor component SCMKB-IIIA3A (130 residues) have been determined. The proteins are mutually homologous and have free threonine as the N-terminal residue and carboxymethylcysteine as the C-terminus. The peptides used for the sequence work were obtained by trypsin, thermolysin, pepsin and chymotrypsin digestions and were fractionated by chromatography on DEAE-cellulose, gel filtration on Sephadex G-25 and G-50, paper chromatography and electrophoresis. The Edman degradation method (employing both the Beckman Sequencer and a non-automatic procedure) was used to obtain the sequences of the peptides.
| S-EPMC1177754 | biostudies-other
Project description:The complete amino acid sequence of protein SCMKB-IIIB4 is presented. It is closely related to the sequence of protein SCMKB-IIIB3 (Haylett, Swart & Parris, 1971) differing in only four positions. The peptic and thermolysin peptides of protein SCMKB-IIIB4 were analysed by the dansyl-Edman method (Gray, 1967) and by tritium-labelling of C-terminal residues (Matsuo, Fujimoto & Tatsuno, 1966). This protein is the third member of a group of high-sulphur wool proteins with molecular weight of about 11400. It consists of 98 residues and has acetylalanine and carboxymethylcysteine as N- and C-terminal residues respectively.
| S-EPMC1176924 | biostudies-other
Project description:The complete amino acid sequence of wool protein SCMKB-IIIB3 was determined. The peptides used for the sequence work were obtained by peptic and thermolysin digestions and were fractionated by chromatography on DEAE-cellulose, paper chromatography and electrophoresis. The peptides were analysed by dansyl-Edman degradation, mass spectrometry and tritium-labelling of C-terminal residues. The protein consists of 98 residues and has acetylalanine as N-terminal residue and carboxymethylcysteine as C-terminus. It is homologous with protein SCMKB-IIIB2 (Haylett & Swart, 1969). A salient feature of the sequence of protein SCMKB-IIIB3 is three consecutive cysteine residues.
| S-EPMC1176923 | biostudies-other
Project description:Fractions corresponding to the S-carboxymethylated high-sulphur protein component SCMK-B2 isolated by Gillespie (1963) from Merino wool were prepared from five different wool samples and also from bovine hair. The six fractions showed great similarities in amino acid composition, and also gave very similar peptide ;maps' after tryptic and chymotryptic digestion. Some of the peptides were isolated from the different samples, and evidence is given that suggests that a sequence of at least 21 amino acids is common to all the fraction SCMK-B2 preparations. Further, all the fractions derived from the wool samples have the same acetylated heptapeptide for the N-terminal sequence, but one extra residue may be present in this N-terminal sequence in the protein from bovine hair. The general significance of these findings is discussed.
| S-EPMC1187197 | biostudies-other
Project description:The importance of sheep's wool in making textiles has inspired extensive research into its structure and the underlying genetics since the 1960s. Wool keratin-associated proteins (KAPs) are a key structural component of the wool fibre. The characterisation of the genes encoding these proteins has progressed rapidly with advances in the nucleotide and protein sequencing. This review describes our knowledge of ovine KAPs, their categorisation into families, polymorphism in the proteins and genes, the clustering and chromosomal location of the genes, some characteristics of gene expression and some potential effects of the KAPs on wool traits. The extent and nature of genetic variation in wool KAP genes and its association with fibre characteristics, provides an opportunity for the development of gene-markers for selective breeding of sheep to produce better wool with properties highly matched to specific end-uses.
| S-EPMC4929423 | biostudies-literature
Project description:We report the extraction of keratin nanofibers from the medulla of a parent yarn after denaturing the cuticle and cortex microstructures of a merino wool yarn. Controlled alkaline hydrolysis, followed by high-speed blending in acetic acid, allowed for the extraction of keratin protein nanofibers with an average diameter of 25 nm and a length of less than 3 μm. SEM and AFM analyses showed the removal of cuticle cells from the yarn. FT-IR and DSC analyses confirmed the hydrolysis and denaturation of the sheet protein matrix of cuticle cells. XPS analysis provided strong evidence for the gradual removal of the epicuticle, cuticle cells, and cortex of the hierarchical wool structure with an increase in alkaline hydrolysis conditions. It was confirmed that the merino wool yarn subjected to hydrolysis under alkaline conditions exposed its internal fibrillar surface. In an acetic acid medium, these fibrillar surfaces obtained a surface charge, which further supported the defibrillation of the structure into its individual nanofibrils during high-speed blending. The extracted nanostructures constitute mainly α-helical proteins. The morphology of the nanofibers is composed of a uniform circular cross-section based on the images obtained using AFM, TEM, and SEM. The extracted nanofibers were successfully fabricated into transparent sheets that can be used in several applications.
| S-EPMC10885782 | biostudies-literature
Project description:A method is reported for the preparation of a group of three proteins from the S-carboxymethylated high-sulphur fraction of wool. These proteins have been partially characterized by their tryptic peptides. All have similar structural features and show an interesting homology within the group and some similarities of sequence with a different group of wool high-sulphur proteins. The evidence for the sequence of some of the peptides is given in a supplementary paper that has been deposited as Supplementary Publication 50008 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1972) 126, 5.
| S-EPMC1173906 | biostudies-other
Project description:Component 7c is one of the four homologous type II intermediate-filament proteins that, by association with the complementary type I proteins, form the microfibrils or intermediate filaments in wool. Component 7c was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage reactions. It is an N-terminally blocked molecule of 491 residues and Mr (not including the blocking group) of 55,600; the nature of the blocking group has not been determined. The predicted secondary structure shows that component 7c conforms to the now accepted pattern for intermediate-filament proteins in having a central rod-like region of approximately 310 residues of coiled-coil alpha-helix flanked by non-helical N-and C-terminal regions. The central region is divided by three non-coiled-coil linking segments into four helical segments 1A, 1B, 2A and 2B. The N-and C-terminal non-helical segments are 109 and 71 residues respectively and are rich in cysteine. Details of procedures use in determining the sequence of component 7c have been deposited as a Supplementary Publication SUP 50152 (65 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257,5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 7c, peptides CN1, CN2 and CN3, and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, (3) details of methods used to determine the C-terminal sequence of peptide CN3, and (4) detailed evidence to justify a number of corrections to the previously published sequence.
| S-EPMC1138930 | biostudies-other
Project description:1. When the diet of sheep is supplemented by the abomasal infusion of sulphur-containing amino acids or casein, a special group of proteins, with a very high content of sulphur (about 8.3%), is incorporated into the high-sulphur proteins of wool. These special proteins cannot be detected in control wool from the same sheep. 2. This is a naturally occurring process, as these special proteins are found in wool from sheep on a high level of nutrition under ordinary conditions of feeding, and in wool of an inherently high sulphur content. 3. This represents a control mechanism in protein synthesis that has not previously been observed, and may be further evidence that the high-sulphur proteins of wool are produced by an unusual synthetic route.
| S-EPMC1264905 | biostudies-other