Results 181 to 190 of about 9,448 (227)
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Differential behavior of gizzard isoactins

Archives of Biochemistry and Biophysics, 1981
Abstract Turkey gizzard smooth muscle myofibrils, the actin of which is composed of 75% smooth muscle γ-isoactin and 25% nonmuscle β-isoactin, were separated into an actomyosin and a cytoskeletal fraction. Isoelectric focusing analysis of the actomyosin actin showed it was 80% γ-isoactin and 20% β-isoactin. It thus appears that the major actin in the
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Chicken gizzard

Anatomy and Embryology, 1985
The fine structure and the organization of muscle and connective tissue in the middle portion of the chicken gizzard (muscular stomach) has been studied by light and electron microscopy. The musculature is divided into long, well-defined bundles arranged circularly and concentrically and extending between the two tendons (tendinous aponeurosis).
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Gizzard Troponin.

Journal of biochemistry, 1976
Native tropomyosin from the gizzard was separated into troponin and tropomyosin. The mode of action of the troponin-tropomyosin system of gizzard was shown to be distinclty different from that of skeletal muscle.
S, Ebashi, T, Toyo-Oka, Y, Nonmura
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Functional morphology of the gizzard of the domestic goose: design of an artificial gizzard

Journal of Zoology, 1998
AbstractAn artificial gizzard was developed to investigate the functional basis of the asymmetry of the gizzard muscles of herbivorous birds, such as the domestic goose (Anser anser). Two types of gizzard muscle morphology were modelled: asymmetric muscles that generated a translational movement; and symmetric muscles that generated a compressional ...
S. J. Moore, C. A. Lill, G. D. Sanson
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The subunit structure of gizzard myosin

Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1973
Gizzard myosin consists of two m ajor subunits, ‘heavy chains’, with chain masses of about 200000 and two minor com ponents ‘light chains’ with chain masses of 20000 and 17000. Quantitative densitometry indicates that the two types of light chains occur in non-stoichiom etric amounts in a myosin molecule, both in purified myosin preparations and in the
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Respiratory Metabolism of Gizzard Shad

Transactions of the American Fisheries Society, 1981
Abstract Rates of oxygen consumption of 48 gizzard shad, Dorosoma cepedianum, were measured in a flow-through respirometer under naturally occurring variations in photoperiod and water temperature. Body length and time of day had little effect on the observed metabolic rates.
Robert J. Pierce   +2 more
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Calcium Regulation in Chicken Gizzard Muscle and Inosine Triphosphate-Induced Superprecipitation of Skeletal Acto-Gizzard Myosin

The Journal of Biochemistry, 1979
Inosine triphosphate (ITP) does not serve as a substrate for myosin light-chain kinase from gizzard muscle. That is to say, myosin light-chain is not phosphorylated in ITP media. Nevertheless, at pH 6.8, 1 mM or 5 mM ITP induces superprecipitation of skeletal acto-gizzard myosin.
H, Onishi, S, Watanabe
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Turkey Gizzard Caldesmon Molecular Weight and Shape

Archives of Biochemistry and Biophysics, 1994
The molecular weight of chicken gizzard muscle caldesmon has been measured previously by sedimentation equilibrium in the analytical ultracentrifuge and found to be 93 +/- 4 kDa [P. Graceffa, C.-L. A. Wang, and W.F. Stafford (1988) J. Biol. Chem. 263, 14196-14202]. The molecular weight of turkey gizzard caldesmon has been determined by another group to
W F, Stafford   +2 more
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Observations on Gizzard Ulcers in Baby Chicks

Avian Diseases, 1968
Because so many gizzard ulcers are found in necropsies of baby chicks, a study was made of this condition. Although the lesions have been called erosions for some time, the majority observed in our work completely perforated the gizzard lining. Bottorff (1) reported observing hemorrhages in the gizzard lining of 18-day embryos in the early 1930's ...
R E, Good, J M, Hetrick, J E, Hanley
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Cation binding to chicken gizzard α-actinin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1994
Gizzard alpha-actinin binds 45Ca2+ as shown by the calcium overlay method. Flow dialysis measurements in 20 mM Hepes (pH 7.5) reveal 3.5 +/- 1.8 (S.D.) high affinity calcium binding sites per dimer, with Kd1 = 6.36 +/- 0.34 x 10(-6) M, and 87.3 +/- 7.2 sites with Kd2 = 1.66 +/- 0.44 x 10(-4) M. Chymotrypsin and thermolysin digestion yielded peptides of
E F, Wenegieme, J A, Babitch, A P, Naren
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