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At least 433 records · Page 24Linked to original sources
PubMed1971

Studies on the high-sulphur proteins of reduced merino wool. Amino acid sequence of protein SCMKB-3B 3 .

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.

Amino Acid Sequence↗
PubMed1971

Studies on the high-sulphur proteins of reduced merino wool. Amino acid sequence of protein SCMKB-3B 4 .

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.

Amino Acids↗
PubMed1972

The amino acid sequence of protein SCMK-B2A from the high-sulphur fraction of wool keratin.

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. 2. This protein of 171 amino acid residues displays both a high degree of internal homology and extensive external homology with other members of the SCMK-B2 group of proteins. 3. Evidence is presented which suggests that the SCMK-B2 group of proteins are produced by separate non-allelic genes.

Amino Acid Sequence↗
PubMed1973

Studies on the high-sulphur proteins of reduced Merino wool. Amino acid sequence of protein SCMKB-3A3.

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.

Amino Acid Sequence↗
PubMed2000

Expression of the homeobox gene, Barx2, in wool follicle development.

We have cloned ovine Barx2, a member of the Bar class of homeobox genes, and present the first description of Barx2 expression in wool follicle development. Barx2 is uniformly expressed in the embryonic ectoderm but is transiently downregulated during the initiation of follicle morphogenesis. Subsequently, Barx2 is expressed throughout the epithelial component of the developing follicle except for a small group of cells at the leading edge of the follicle placode. These Barx2-negative cells are destined to form the follicle bulb and are the progenitors of the inner root sheath and hair shaft. In adult follicles, Barx2 is expressed throughout the outer root sheath but not in the inner root sheath or hair shaft, or in dermal cells associated with the follicle. The pattern of Barx2 expression in follicle morphogenesis is similar to that of the cell adhesion molecule E-cadherin, a similarity that echoes Barx2 coexpression with the L1 cell adhesion molecule in other tissues during mouse embryogenesis. Barx2 is also expressed in tongue and esophagus, two other keratinizing tissues, and we speculate that Barx2 may have a general function in controlling adhesive processes in keratinizing epithelia.

Animals↗
PubMed1976

Preparation of metabolically active cell suspensions from wool roots.

A method is described for the preparation of metabolically active cell suspensions from plucked wool roots using the proteolytic enzyme trypsin. The suspensions consist of a heterogeneous population of cells which appear similar in morphology to follicle bulb cells, differentiating keratinocytes and possibly cells of the inner root sheath. The concentrations of trypsin and of inorganic ions for optimum activity of the suspensions have been determined, and the inclusion of EGTA was found to increase the yield of cells. The cell suspensions incorporate [14C]leucine, [3H]uridine and [3H]thymidine into acid-insoluble products, and are sensitive to the action of cycloheximide and emetine, but not to chloramphenicol or rifampin. Autoradiography has shown that the cells believed to be derived from the follicle bulbs show the greatest activity.

Animals↗
PubMed1976

Location of a high-sulphur protein in developing wool follicles using peroxidase-labelled antibody.

Antiserum to a high-sulphur protein (SCMK-B2) from wool was purified to obtain the immunoglobin G fraction, and this was labelled with horse-radish peroxidase. The labelled antibody was then applied to sections of sheep skin embedded in glycol methacrylate in order to locate the distribution of high-sulphur protein within the lower hair shaft. Regions containing the highest concentration of high-sulphur protein were the cuticle of the hair shaft and the keratogenous zone of the cortex.

Animals↗
PubMed1980

Migration and keratinization of cells in wool follicles.

Migration of cells in wool follicles of an adult Merino sheep was studied autoradiographically in skin samples taken at intervals after an intravenous injection of [3H]thymidine. Fibre and inner root sheath cells incorporated [3H]thymidine in a cone-shape region of the follicle bulb. Labelled inner sheath cells migrated out of the bulb ahead of contemporaneous cells in the fibre and remained in advance, although to a progressively lesser extent, until the inner sheath cells sloughed into the follicle lumen. Outer root sheath cells incorporated [3H]thymidine along the length of the follicle. Cells in the proximal half of the outer sheath migrated inwards and distally and sloughed into the follicle lumen before contemporaneous inner sheath cells. Other cells in the distal half of the outer sheath migrated past the level where cells from the proximal population were shed and also sloughed into the lumen. In the most distal part of the outer sheath, which formed the epidermis-like lining of the follicle canal, little migration of cells was observed during 8 days of observation. The specific activity of tritium in fibres plucked from the same sheep at intervals after the intravenous injection of [3H]thymidine was determined by scintillation counting and assessed in terms of cell migration and hardening of the fibres. The time which the specific activity of solvent-degreased fibres reached a maximum was found to give an estimate of the time for cells in the fibre to migrate to the upper limit of the keratogenous zone. When the plucked fibres were extracted with 8 M urea the times of the maximum specific activities of the urea-dispersible and urea-insoluble material provided respectively estimates of the times at which hardening of the fibres began and ended. The effects of different planes of nutrition were examined in two other Merino sheep by radioassay of fibres plucked after intravenous injections of [3H]thymidine given after equilibration period of at least 2 months on each level of feeding. A high plane of nutrition the rate of cell migration and hastened the onset of hardening of the fibres, but prolonged the hardening process. The prolongation of the hardening process was confirmed by the specific activities of fibres plucked after intravenous injections of [35S]cystine.

Animals↗
PubMed1986

Mitotic activity in cells of the wool follicle bulb.

Mitotic activity in the cells of the germinative region of wool follicle bulbs was quantified by using small (0.1-0.5 ml) intradermal doses of colchicine and selective staining of the metaphase-blocked nuclei using either crystal violet, iodine and eosin or haematoxylin and eosin. The number of metaphase nuclei present 3 h after colchicine administration increased with colchicine dose from 0 to 1 microgram and thereafter remained relatively constant up to 200 micrograms colchicine. The accumulation of metaphase nuclei was linear for up to 6 h after intradermal colchicine. The metaphase-blocking effect of intradermal colchicine was confined to a radius of less than 5 cm from the injection site, allowing a number of estimates of mitotic rates to be made over a small area of skin. Such estimates revealed little variation in mitotic activity over the midside region of the sheep, although there were substantial differences in follicle activity at different sites over the body. The technique is simple, allows serial or concurrent estimates of mitotic activity to be made in the same animal, and eliminates problems associated with intravenous colchicine administration. It was used to derive the relationship between follicle activity and fibre production after nutritional changes, and to define the time course of mitotic events after administration of the antimitotic defleecing agent cyclophosphamide.

Animal Nutritional Physiological Phenomena↗
PubMed1984

The influence of urea diet supplemented with protected protein on metabolism and wool growth in sheep.

The utility of blood meal and formaldehyde treated casein as protein supplements in the nutrition of sheep receiving approximately 50% of their total nitrogen from urea was studied. It was observed that protected protein supplements positively influenced wool growth and quality. On the basis of biochemical analysis of blood the mechanism of this effect is discussed. It seems that small protein supplements (about 6% of the total protein) are not only a source of amino acids in the duodenum but also influence the hormonal control in animals.

Amino Acids↗
PubMed1992

[Relationship between wool yield and cyst(e)ine level in blood plasma].

Publications from Williams were the stimulation to study the relations between wool yield and cyst(e)ine concentration in blood plasma. Methodical experiments were carried out and the two methods used each provided clear results. At the same time the reversible binding of a part of the free cystine in the plasma with the plasma proteins and its effect on the analysis results might be considered. After an interpretation of the two methods their use is described taking into consideration the factors influencing the results of the analysis. It is concluded that the two methods are usable for the planned purpose.

Animals↗
PubMed2004

Feasibility analysis of in-plant control for water minimization and wastewater reuse in a wool finishing textile mill.

This study evaluates the feasibility of water minimization and wastewater reuse for a wool finishing textile mill. The evaluation process is based upon a detailed analysis on water use, process profile and wastewater characterization, indicating a potential for 34% reduction in water consumption and for 23% of wastewater recovery for reuse. Wastewater reuse requires treatment and results in a remaining wastewater stream with stronger character and consequently more costly to treat. The feasibility includes technical considerations for appropriate treatment alternatives and related cost factors for water consumption, treatment for reuse and for discharge either to sewer or to receiving media.

Animals↗
PubMedDate not supplied

Electron spin resonance spectrometrical study of the melanins in the wool of some North European sheep in relation to their color inheritance.

Additional peaks that were known on the esr-spectrograms of red human and reddish-brown Karakul hair to be diagnostic traits of phaeomelanin esr-signal also were found on esr-spectrograms of the tan, but not of black or chocolate brown wool from Icelandic sheep. This tan color is thought to depend on the presence of phaeomelanin and is due to the top dominant allele at the A locus. The two methods of distinguishing between eu- and phaeomelanin-dependent brown colors--esr-spectrometrical and genetical--are in agreement for European as well as for Asiatic breeds. Both light and dark brown Soay fleece samples lacked the additional peaks and are interpreted as eumelanin pigmentation.

Animals↗
PubMed1989

Respiratory allergy and specific immunoglobin E and immunoglobin G antibodies to reactive dyes used in the wool industry.

Respiratory symptoms among six employees in wool dye-houses in the United Kingdom were investigated. Clinical histories revealed that all had work-related respiratory symptoms, which they associated with exposure to Lanasol dyes. Five of the six subjects had specific Immunoglobin E to human serum albumin conjugates of one or more of the dyes to which they were exposed, providing evidence of sensitization to these dyes. In two subjects there was a definite association between symptoms to a particular dye, and specific IgE to an albumin conjugate of that dye. Specific IgG was found in exposed subjects, irrespective of the presence of allergic symptoms, indicating that specific IgG reflects exposure rather than clinical sensitization. Four of the six subjects had specific IgG4; this was only present in the subjects with respiratory allergy and specific IgE.

Adult↗
PubMed1985

Epidermal hyperplasia and wool follicle regression in sheep infused with epidermal growth factor.

The proliferative activities of germinative cells of the wool follicles and the epidermis have been determined in sheep treated with epidermal growth factor (EGF). Infusions of 0.17-0.72 mg EGF/kg metabolic body weight (MBW) for 28 h resulted in marked declines in the mitotic indices (MI) of the follicle bulb cell populations 24 h after the beginning of treatment, the lowest values being recorded at 48 h. Follicular activity subsequently recovered and the MI returned to preinfusion levels after 3-8 days. The inhibition of fiber production resulting from the decline in bulb cell division caused the development of a break in the fleece. By contrast, the MI of the peripheral cells of the sebaceous gland acini and the basal cells of the epidermis increased after EGF treatment, reaching peaks 48-72 h after the beginning of infusion. The degree to which all of these responses were observed appeared to be approximately correlated with the amount of EGF administered.

Animals↗
PubMed1994

Characterization of a hair (wool) keratin intermediate filament gene domain.

In epithelial differentiation keratin intermediate filament genes are expressed in multifarious tissue-specific and stage-specific patterns. Pairs of type I and type II intermediate filament genes, belonging to multigene families, are coordinately regulated, and 4-5 genes of each type are expressed in the hair follicle. Accumulating chromosomal mapping data points to a major locus for each intermediate filament multigene family on separate chromosomes. In this report we describe the isolation of a sheep hair keratin cosmid by chromosome walking that overlaps two previously described cosmids and establishes a continuous 100-kb segment of cloned DNA containing three hair and three hair-like type II intermediate filament keratin genes. A new hair keratin type II intermediate filament gene, KRT2.11, is located in the middle of the cluster, and partial sequence data reveal a striking conservation of its predicted N-terminal region with other sheep hair keratin type II intermediate filament proteins. Expression analyses demonstrate the presence of a 2.4-kb KRT2.11 transcript in wool follicle RNA and show that expression occurs in the follicle cortical keratinocytes above the dermal papilla. The three hair genes are clustered within about 40 kb and flanked by hair-like genes that are not expressed in the hair follicle, thereby demarcating a hair keratin gene domain.

Amino Acid Sequence↗
PubMed1994

Polymorphism in two genes for B2 high sulfur proteins of wool.

Variation in the nucleotide sequence of the B2 high-sulfur protein genes has not been reported previously. This paper reports 15 nucleotide substitutions in each of the genes for the B2A and B2C proteins and a length of polymorphism in the B2A gene which translates to the insertion/deletion of one 30-nucleotide repeat sequence. Evidence is presented for gene conversion occurring within the B2 high-sulfur multigene family. These DNA polymorphisms may account for some of the microheterogeneity observed in the B2 high-sulfur proteins and may also be useful genetic markers of the B2 high-sulfur protein gene loci for future use in analysing wool fibre characteristics.

Alleles↗
PubMed1976

Banked blood microfiltration. II. Dacron-wool microfilter.

It is well established that debris tends to accumulate in banked blood, the amount of debris increasing with storage time. If such a blood is transfused to a patient, it will be filtered by the capillary network of the lungs and could cause various intensities of microemboli. These can be prevented by microfiltration--the Swank IL200 transfusion filter made of Dacron wool is perfectly suitable. It removes more than 70% of the debris 29-100 mum size from four blood units and its efficiency for particle removal is greatly increased by lactate priming.

Animals↗