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Feather, feathers

The feather is thought to have evolved from the scaly skin of reptiles. Long scales with frayed outer edges may gradually have developed into more and more complex and useful structures, and may eventually have become feathers. Feathers are rare in the fossil record. They are found as fragments in... [Pg.131]

Chicken feathers can be converted to fibers for use in diapers.140 Each chicken produces 0.5 1.0 lb of feathers. Feathers, hides, hoofs, and hair all contain proteins containing cystine cross-links. Cured rubber containing disul-... [Pg.374]

In 1998, Wolkers et al. [73] identified changes in the protein secondary structure in association with desiccation tolerance of developing maize embryos by SR-IMS. The same technique was used by Yu et al. for comparison of the protein secondary structure of various grains with those of feathers. Feathers contain more than 80% of -folded protein, whereas grain is mainly composed of a-helix structured protein that is located in higher concentrations only in the endosperm [63, 74]. [Pg.250]

Waxes are water repelling solids that are part of the protective coatings of a number of living things including the leaves of plants the fur of animals and the feathers of birds They are usually mixtures of esters m which both the alkyl and acyl group are unbranched and contain a dozen or more carbon atoms Beeswax for example contains the ester triacontyl hexadecanoate as one component of a complex mixture of hydrocar bons alcohols and esters... [Pg.1079]

Wax (Section 26 5) A mixture of water repellent substances that form a protective coating on the leaves of plants the fur of animals and the feathers of birds among other things A principal component of a wax is often an ester in which both the acyl portion and the alkyl portion are characterized by long carbon chains... [Pg.1296]

I remember snow, Soft as feathers, Sharp as thumb tacks,.. . ... [Pg.345]

Birch leaf extract Birch reduction Birch-type reactions Bird feathers Bird repellents Bireactive dyes Birkeland-Eyde process Birnessite [1244-32-5] b-Bisabolene [495-61-4]... [Pg.110]

In the United States, more than 16.3 x 10 kg of human-inedible raw materials are available each year, and the rendering industry is a valuable asset in diverting these into valuable ingredients for use primarily in animal foods (4). The three largest meat packers are responsible for nearly four-fifths of aU red meat production (5) and enormous amounts of rendered meat meal and animal fat. Three broiler producers account for about 40% of the total broiler production. American Proteins, Inc. (RosweU, Georgia), the world s largest processor of poultry by-products, produces more than 450,000 t of poultry meal, feather meal, and poultry fat each year. It also produces more than 100,000 t of fish meal, fish oil, and fish products each year. Pish meal production worldwide in 1986 was estimated at 6.23 x 10 t, which with the 125 x 10 t of meat and bone meal plus 6.67 x 10 t of feather meal and poultry by-product meal (6) is the primary source of animal proteins used by the pet food industry. [Pg.150]

Eeather meal, first hydroly2ed and then oxidi2ed, produces cysteic acid [13100-82-8] an excellent precursor for taurine in cats (20). Hydroly2ed feather meal may supplement the taurine provided by other dietary animal proteins and help replace part or all of the synthetic taurine in cat food formulations with considerable cost savings. [Pg.151]

American Association of Textile Chemists and Colorists P.O. Box 12215 Research Triangle Park, NC 27709 Inter-Society Color Council U.S. Army Natick R D Center Att STRNC-ITC Natick, Mass. 01760 Friction Materials Friction Materials Standards Institute E210, Route 4 Paramus, NJ 07652 Feather Tanners Council of America 2501 M Street, NW Washington, D.C. 20037... [Pg.25]

Production by Isolation. Natural cysteine and cystine have been manufactured by hydrolysis and isolation from keratin protein, eg, hair and feathers. Today the principal manufacturing of cysteine depends on enzymatic production that was developed in the 1970s (213). [Pg.291]

G. R. Waller and M. S. Feather in The Maillard Reaction in Foods and Nutrition, American Chemical Society, Washington, D.C. 1983 F. Hata and M. Oimomi, Rinsho KensaSS, 893 (1989). [Pg.299]

Wool belongs to a family of proteins, the keratins, that also includes hair and other types of animal protective tissues such as horn, nails, feathers, and the outer skin layers. The relative importance of wool as a textile fiber has declined over the decades as synthetic fibers have increa singly been used in textile consumption. Wool is still an important fiber in the middle and upper price ranges of the textile market. It is also an extremely important export for several nations, notably AustraUa, New Zealand, South Africa, and Argentina and commands a price premium over most other fibers because of its outstanding natural properties of soft handle (the feel of the fabric), moisture absorption abiUties (and hence comfort), and superior drape (the way the fabric hangs) (see Fibers Textiles). Table 2 shows wool production and sheep numbers in the world s principal wool-producing countries. [Pg.338]

Wool, as a keratin, is a highly cross-linked, insoluble proteinaceous fiber, and few animals have developed the specialized digestive systems that aUow them to derive nutrition from the potential protein resource. In nature, these few keratin-digesting animals, principally the larvae of clothes moths and carpet beetles, perform a useful function in scavenging the keratinous parts of dead animals and animal debris (fur, skin, beak, claw, feathers) that ate inaccessible to other animals. It is only when these keratin-digesting animals attack processed wool goods that they are classified as pests. Very often they enter domestic or industrial huildings from natural habitats such as birds nests. [Pg.349]

J. Christner, "The Use of Lipases ia the Beam House Processes," paper preseated at the S7th American Feather Chemists Association s Annual Meeting Waterville Valley, N.H.,]uae 1991. [Pg.305]

For inlet or outlet end erosion-corrosion, either extend tube ends 3 or 4 inches into the water box or install sleeves, inserts, or ferrules into the tube ends. These should be a minimum of 5 inches long. The ferrules may be nonmetallic or erosion-resistant metals, such as stainless steel, if galvanically compatible. The end of the ferrule should be feathered to prevent turbulence. [Pg.249]

Fig. 28.7. Modification to remove attachment weld from surface of shaft. The collar con be pressed on to the shaft and secured with o feather key, but we must remember that the keywoy will weaken the shaft. Fig. 28.7. Modification to remove attachment weld from surface of shaft. The collar con be pressed on to the shaft and secured with o feather key, but we must remember that the keywoy will weaken the shaft.
Alpha helices are sufficiently versatile to produce many very different classes of structures. In membrane-bound proteins, the regions inside the membranes are frequently a helices whose surfaces are covered by hydrophobic side chains suitable for the hydrophobic environment inside the membranes. Membrane-bound proteins are described in Chapter 12. Alpha helices are also frequently used to produce structural and motile proteins with various different properties and functions. These can be typical fibrous proteins such as keratin, which is present in skin, hair, and feathers, or parts of the cellular machinery such as fibrinogen or the muscle proteins myosin and dystrophin. These a-helical proteins will be discussed in Chapter 14. [Pg.35]

The rectangular element valve, as the name implies, uses rectangular-shaped sealing elements. These valves are the feather valve, channel valve, and the reed valve. These valves are applied to the industrial air machines for the most part. A channel valve is shown in Figure 3-10. [Pg.70]


See other pages where Feather, feathers is mentioned: [Pg.31]    [Pg.466]    [Pg.858]    [Pg.192]    [Pg.223]    [Pg.453]    [Pg.31]    [Pg.466]    [Pg.858]    [Pg.192]    [Pg.223]    [Pg.453]    [Pg.230]    [Pg.356]    [Pg.179]    [Pg.141]    [Pg.17]    [Pg.19]    [Pg.313]    [Pg.413]    [Pg.116]    [Pg.251]    [Pg.336]    [Pg.248]    [Pg.417]    [Pg.423]    [Pg.423]    [Pg.298]    [Pg.303]    [Pg.440]    [Pg.443]    [Pg.446]    [Pg.381]    [Pg.185]    [Pg.172]    [Pg.287]   
See also in sourсe #XX -- [ Pg.4 ]




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Birds feathers

Chemical analysis of feather and down textile materials

Chick embryos feathers

Chicken feather fibres

Chicken feather protein hydrolysate

Contour feathers

Duck feathers

Feather alum

Feather amino acid composition

Feather and down textiles

Feather bombs

Feather color

Feather edge

Feather extraction

Feather fibres

Feather hydroids

Feather keratins

Feather keratins 3-sheet structure

Feather meal

Feather parts

Feather pecking

Feather protein

Feather sequence studies

Feather structure

Feather thermal conductance

Feather types

Feather wrapping

Feather-like nanostructures

Feathered Men

Feathered Wing feather section

Feathered Wing roof structure

Feathered wing, Feuchtwangen

Feathering

Feathering

Feathering method

Feathering technique

Feathers

Feathers

Feathers, contact angle

Feathers, grading

Flight feathers

Glass-feather manometer

Hydrolyzed poultry feathers

Peacock feathers

Poultry feather pecking

Powder feathers

Proteins keratin, feather

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