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At least 217 records · Page 12Linked to original sources
PubMed1996

Kinetic disposition of an aqueous formulation of alphacypermethrin applied to the dorsal mid-line of sheep with long wool and its effect on lice.

A group of 5 adult Merino sheep with fleeces about 70 mm long (7-months growth of wool) was treated with a topical formulation of the synthetic pyrethroid insecticide, alphacypermethrin, applied to the dorsal mid-line. Insecticide concentrations at the tip, middle and base of wool staples collected from meridians along the back, upper and lower flanks were measured at intervals from 1 to 98 days after treatment. Some movement of the alphacypermethrin from the back to the lower body occurred within 24h after treatment, but despite careful application of the insecticide there was wide variation in the concentration between and within meridians. The majority of the alphacypermethrin remained close to the dorsal mid-line and near the tip of the staple. There were significant differences in the concentration between the tip, middle and base segments of the staples in the back and lower flank meridians (P < 0.05). Despite exposure of the sheep to normal weathering, there was no significant difference in the concentration of alphacypermethrin between samples collected at day 1 or day 98 after treatment (P > 0.05). Numbers of pyrethroid-susceptible lice surviving exposure in vitro for 20 h differed significantly between samples collected at different times after treatment, lice survived for 20 h in wool taken from parts of the fleece that contained high (P < 0.05). The numbers of lice surviving in samples collected within 28 days after treatment tended to be lower than in those collected from 28 to 98 days but, in some samples, regardless of time after treatment, concentrations of alphacypermethrin.

Administration, Topical↗
PubMed1997

Mycological and some physiological studies of keratinophilic and other moulds associated with sheep wool.

Wool samples of 50 healthy sheep collected from different localities at Ar' Ar in Saudi Arabia were examined for the presence of keratinophilic and other fungi using the hair plate technique. Forty-eight species and 2 varieties belonging to 20 genera were isolated on Sabouraud's dextrose agar at 25 degrees C. Two species of true dermatophytes were isolated: Trichophyton terrestre and T. rubrum in low frequency of occurrence. Chrysosporium, a well-know keratinophilic genus, was the predominant genus on sheep wool. Of 6 Chrysosporium species isolated C. tropicum, C. keratinophilum and C. indicum were the most prevalent. Several other moulds could colonize wool, and the most frequent species were members of the genera Aspergillus, Penicillium, Emericella, Chaetomium and Acremonium. 14 isolates of selected fungi were screened for their ability to produce protease and keratinase on solid media. All test fungi exhibited protease, but with varying degree. It was observed that true dermatophytes Trichophyton rubrum, T. terrestre and the keratinolytic fungi Chrysosporium tropicum and C. keratinophilum showed highly keratinolytic activity, but Emericella nidulans var. lata, E. quadrilineata and Penicillium funiculosum were not able to attack horse hair.

Animals↗
PubMed2003

Proteomic database of wool components.

The separation, classification and identification of wool fibre proteins has been of interest for many years. The purposes of this review are to summarise past work in this area and to evaluate the application of modern proteomic techniques to the identification and characterisation of wool proteins. The current state of knowledge of the wool proteome will also be presented.

Amino Acid Sequence↗
PubMedDate not supplied

Water absorbency by wool fibers: Hofmeister effect.

Wool is a complex material, composed of cuticle and epicuticle cells, surrounded by a cell membrane complex. Wool fibers absorb moisture from air, and, once immersed in water, they take up considerable amounts of liquid. The water absorbency parameter can be determined from weight gain, according to a standard method, and used to quantify this phenomenon. In this paper we report a study on the water absorbency (or retention) of untreated wool fibers in the presence of aqueous 1 M salt solutions at 29 degrees C and a relative humidity of either 33% or 56%. The effect of anions was determined by selecting a wide range of different sodium salts, while the effect of cations was checked through some chlorides and nitrates. Our results show a significant specific ion and ion pair "Hofmeister" effects, that change the amount of water absorbed by the fibers. To understand this phenomenon, the water absorbency parameter (A(w)) is compared to different physicochemical parameters such as the lyotropic number, free energy of hydration of ions, molar surface tension increment, polarizability, refractive index increment, and molar refractivity. The data indicate that this Hofmeister phenomenon is controlled by dispersion forces that depend on the polarizability of ionic species, their adsorption frequencies, the solvent, and the substrate. These dispersion forces dominate the behavior in concentrated solutions. They are in accord with new developing theories of solutions and molecular interactions in colloidal systems that account for Hofmeister effects.

Absorption↗
PubMed2003

Recycled wool-based nonwoven material as an oil sorbent.

The aim of this study was to highlight the possibility of using recycled wool-based nonwoven material as a sorbent in an oil spill cleanup. This material sorbed higher amounts of base oil SN 150 than diesel or crude oil from the surface of a demineralized or artificial seawater bath. Superficial modification of material with the biopolymer chitosan and low-temperature air plasma led to a slight decrease of sorption capacity. Loose fibers of the same origin as nonwoven material have significantly higher sorption capacities than investigated nonwoven material. White light scanning interferometry analysis of the fibers suggested that roughness of the wool fiber surface has an important role in oil sorption. The laboratory experiments demonstrated that this material is reusable. Recycled wool-based nonwoven material showed good sorption properties and adequate reusability, indicating that a material based on natural fibers could be a viable alternative to commercially available synthetic materials that have poor biodegradability.

Adsorption↗
PubMed1968

Evidence of homology in a high-sulphur protein fraction (SCMK-B2) of wool and hair alpha-keratins.

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.

Animals↗
PubMed1972

The amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin.

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.

Amino Acid Sequence↗
PubMed1974

The reactivity of the disulphide bonds of wool.

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.

Alkylation↗
PubMed1992

Type II intermediate-filament proteins from wool. The amino acid sequence of component 5 and comparison with component 7c.

Component 5 is one of the four type II intermediate-filament proteins found in the hard keratin wool. It 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. Component 5 is an N-terminally blocked molecule of 503 residues and Mr (not including the blocking group) of 56,600. The blocking group has not been identified. The amino acid sequence of component 5 shows 77% sequence identity with that of component 7c, another type II wool intermediate-filament protein [Sparrow, Robinson, McMahon & Rubira (1989) Biochem. J. 261, 1015-1022]. The sequence similarity extends from the N-termini of the two molecules to residue 459 (component 5 sequence); however, there is no recognizable sequence similarity in the remaining C-terminal 43 amino acid residues. Details of procedures used in determining the sequence of component 5 have been deposited as a Supplementary Publication SUP 50168 (80 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. (1992) 281, 5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 5, peptide CN1, the peptide mixture CN2/3 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, and (3) details of the method used to determine the C-terminal sequence of component 5.

Amino Acid Sequence↗
PubMed1975

Studies on the inhibition of synthesis of the tyrosine-rich proteins of wool.

Three treatments known to produce weak wool were imposed on sheep, and the effects on the synthesis of high-tyrosine wool proteins were noted. The treatments were: intravenous infusion of the amino acid mimosine (a potential chemical defleecing agent), intravenous injection of the synthetic steroid Opticortenol (dexamethasone-21-trimethylacetate), and the abomasal infusion of methionine into sheep consuming a diet of wheat. All three treatments caused a partial suppression of high-tyrosine protein synthesis. The inhibition caused by mimosine could not be prevented by the simultaneous infusion of tyrosine or phenylalanine, suggesting that in this system mimosine is not acting as a tyrosine antagonist. The role of phenylalanine in controlling the synthesis of the high-tyrosine proteins in wool was also investigated. Although the infusion of an amino acid mixture minus phenylalanine reduces the level of these proteins, supplements of phenylalanine or tyrosine do not stimulate their synthesis, irrespective of the initial level in the fibre. The improtance of aromatic amino acids in the regulation of the high-tyrosine proteins is therefore uncertain. Suppression of the high-tyrosine proteins is usually accompanied by a stimulation in the synthesis of the ultra-high-sulphur proteins, although there does not seem to be a simple stoichiometric relationship between the two protein types.

Amino Acids↗
PubMed1975

Influence of nutrition on the crimping rate of wool and the type and proportion of constituent proteins.

When the nutritional level of sheep is restricted, the staple crimp frequency of the resultant fleece increases substantially whereas the cystine and high-sulphur protein contents decrease. This is in marked contrast to the direct relationship between crimp frequency and cystine content among sheep. These observations can be reconciled by assuming that variations in crimp frequency are attributable solely to a combination of follicle shape and fibre length growth rate without recourse to the more generally accepted theories relating to the proportion and distribution of ortho- and paracortical cells in the firbre cortex. The major portion of the decrease in the cystine content of high-crimp wools is due to the decreased synthesis of a specific protein fraction (ultra-high-sulphur protein) as would be expected from the results of dietary supplementation experiments. Low-crimp wools do not appear to contain this protein fraction and in this respect they may differ from high-crimp wools.

Amino Acids↗
PubMed1976

Inhibition of wool follicle DNA synthesis by mimosine and related 4(1H)-pyridones.

The in vitro incorporation of [3H]thymidine has been examined in thin slices of sheep skin. Most of the radioactivity (88%) was incorporated into the bulb cells of the wool follicles, and the technique is therefore suitable for the study of some aspects of wool follicle DNA synthesis. The effect of mimosine and a number of related 4(1H)-pyridones on [3H]thymidine incorporation into sheep skin slices was examined. Mimosine was shown to inhibit the incorporation at a concentration of 0-2 mM. At this concentration, the incorporation of [3H]uridine or [14C]leucine was not affected. The inhibition of [3H]thymidine incorporation was time dependent, 2 h of incubation being required for maximal inhibition of DNA synthesis, and was readily reversible by removal of mimosine from the incubation medium. The 3-hydroxyl-4-oxo function of the pyridone ring appears to be directly involved in DNA synthesis inhibition. The amino acid side chain is not a toxophoric centre, but changes in its polarity have been shown to affect the inhibitory activity. The results suggest that the primary action of mimosine on the inhibition of wool biosynthesis in vivo is the inhibition of follicle bulb cell DNA synthesis and consequently of cell division.

Animals↗
PubMed1979

Cell proliferation and cortical cell production in relation to wool growth.

The relationship of wool growth to cell proliferation in the follicle bulb and to the subsequent migration and growth of the fibre cortical cells was investigated in 10 Peppin Merino sheep. These sheep had been maintained on a low, medium or high level of nutrient intake to ensure a wide range in wool growth. The number and mitotic activity of the germinal cells in the follicle bulb were determined after administration of colchicine. Cortical cell size was measured following isolation of the fibre cells by acid-treatment of wool. The average fibre production of the follicle varied from 4.1 x 10(4) to 13.2 x 10(4) micron3/day in these sheep. There were also substantial differences between sheep in the mitotic activity of the germinal cells in the bulb, the rate of cell proliferation being highly correlated with the average daily fibre production of the follicle (r = + 0.88, n = 10). However, the size of the germinal cell population differed from sheep to sheep and was not closely related to the level of fibre production (r = + 0.48, n = 10). The average turnover time of these cells was inversely related to fibre production and varied from 41.6 to 19.4 h (r = -0.82, n = 10). Multiple regression analysis of the data showed that the average daily fibre production of the follicle was largely determined by the number of germinal cells present in the bulb and their rate of proliferation (R = +0.95, n = 10). Variations in cell turnover time and in cortical cell size were not significant in influencing the rate of fibre production. In these sheep, the average cortical cell varied in size from 658 to 1279 micron 3 and the positive correlation (r = + 0.83, n = 10) found between cell size and fibre production is considered to merely reflect an allometric relationship. The proportion of germinal cells contributing to the fibre cortex was found to be small and variable, ranging from 9.4 to 17.8%. Furthermore, this proportion was not related to the nutritional level of these sheep, and it is thought that the variability in the distribution of cells to the fibre may be attributed to genetic differences between sheep.

Animals↗
PubMed1980

Effects of internally administered N-[5-(4-aminophenoxy)pentyl]phthalimide on wool follicles and skin of sheep.

When N-[5-(4-aminophenoxy)pentyl]phthalimide was administered to sheep in sufficient quantities to permit manual removal of the fleece (400 mg/kg body weight orally, or 75 mg/kg body weight intravenously during a period of 48 h), cell division ceased in the wool follicle bulbs within 1 day. Dark-staining bodies (autophagic vacuoles) developed concomitantly in the cytoplasm of the bulb cells. The nuclei of cells in the keratogenous zones of the fibres became pycnotic 2 days after dosing and subsequent keratinization of these portions of the fibres was impaired. All the follicles retrogressed prior to day 7 after dosing, and the root ends which formed on the fibres moved towards the skin surface, reaching the level of the sebaceous glands by day 7. At this time mitotic activity recommenced around the dermal papillae in about 50% of the follicles. A small number of tips of new fibres emerged from the skin surface of some of the depilated sheep by day 14. The root ends on the fibres in the fleeces harvested at days 7-15 were fragmented with various degrees of taper. By 21 days, most follicles were growing emergent fibres. Thickening of the epidermis, increase in sebaceous gland size and decrease in skin thickness occurred in some of the depilated sheep. Smaller doses of the compound (200 mg/kg body weight orally or 40 mg/kg body weight intravenously during 24 h) produced weakness in the wool. Fewer autophagic vacuoles were present in follicle bulbs 1 day after dosing and not all follicles regressed. The weakened region of the fleece contained a mixture of shed fibre ends and continuously growing fibres with thin regions proximal to poorly keratinized lengths of fibre. No change was observed in other components of the skin of the sheep with weakened wool. The follicular changes produced by this compound are similar in some respects to those produced by other depilatory compounds or that occur during natural cyclic hair growth.

Animals↗
PubMed1984

Further studies on the effects of the presence or absence of protozoa in the rumen on live-weight gain and wool growth of sheep.

Lambs were given a diet of oaten chaff-sucrose-fishmeal (48:48:4, w/w) and either 60 (diet A) or 120 (diet B) g urea/kg sucrose in the diet. All animals were defaunated and half were refaunated. Each group of lambs (faunated and defaunated) was then divided into two groups and given diet A or diet B. Feed intake, wool growth and live-weight change were monitored over a 182 d period. The level of urea supplementation had no effect on wool growth or live-weight gain. Defaunated lambs gained live weight at a higher rate (9%, P less than 0.06) and grew 37% more wool (P less than 0.01) than the lambs with large populations of protozoa in their rumens.

Animals↗
PubMed2003

Variation of pH, conductivity and potential values in chromium (VI) removal by wool.

Variation of pH, conductivity and potential values in chromium (VI) removal by wool was investigated in this study. In addition to chromium (VI) concentrations, pH, conductivity and potential values were also traced during the experimental studies. After applying linear regression to experimental data, it was seen that there was a relationship between pH, conductivity, potential values and chromium (VI) concentrations in the aqueous solution after treatment with wool. This relationship was evaluated in the light of the analyses of the linear regression. Kinetic data and adsorption isotherms for chromium (VI) adsorption by wool were also determined.

Adsorption↗
PubMed1975

Filtration characteristics of dacron wool (Swank) blood transfusion filters.

Stored human blood of varying age was passed through standard commercial blood transfusion filters (pore size, 170 mu) and Swank Dacron wool blood transfusion filters (pore size, 20mu). Passage through the Dacron filter resulted in a marked decrease in SFP and an increase in filter weight indicating removal of microaggregates which have been implicated as a cause of pulmonary insufficiency. The commercial filter tested did not appear to be effective in removing these harmful aggregates. On the basis of this research it is concluded that the Swank Dacron wool blood transfusion filter will prevent pulmonary microemboli during transfusion. Because aggregate removal appeared to be quantitative, it is recommended that no more than four units of blood be passed through each Dacron wool filter.

Animals↗
PubMed1980

The isolation of wool keratin messenger RNA from sheep.

A method for the isolation of polysomal RNA from plucked wool follicle tissue is described. When translated in a reticulocyte lysate cell-free system, the products encoded by the RNA are electrophoretically identical to the low-sulfur and high-sulfur wool keratins. Since non-keratin translation products were not detected, the keratin mRNA species appear to be the predominant messenger component of the polysomal RNA. Sucrose gradient fractionation of the polysomal RNA gave rise to 2 discrete peaks of keratin mRNA, with mean sizes of 21S and 11S. The 21S fraction coded for the low-sulfur and larger high-sulfur wool keratins, while the 11S fraction coded for proteins smaller than about 20000 daltons, possibly the high-tyrosine keratins and smaller high-sulfur keratins. The keratin mRNA can be separated from the bulk ribosomal RNA by oligo(dT) cellulose chromatography, and hence is presumed to contain a terminal poly(rA) tract.

Animals↗