Results 171 to 180 of about 9,448 (227)
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Archives of Biochemistry and Biophysics, 1966
Abstract The Ca++-ATPase activity of chicken gizzard myosin is increased 2- to 3-fold by tryptic treatment and by various substances, urea, guanidine-HCl, sodium dodecylsulfate, KCNS, LiBr, ethanol, or ethylene glycol. These substances also activate the Ca++-ATPase of rabbit uterus myosin but have no effect on the Ca++-ATPase of chicken breast myosin.
M, Bárány +3 more
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Abstract The Ca++-ATPase activity of chicken gizzard myosin is increased 2- to 3-fold by tryptic treatment and by various substances, urea, guanidine-HCl, sodium dodecylsulfate, KCNS, LiBr, ethanol, or ethylene glycol. These substances also activate the Ca++-ATPase of rabbit uterus myosin but have no effect on the Ca++-ATPase of chicken breast myosin.
M, Bárány +3 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
Abstract 1. 1.Chicken gizzard Subfragment 1 was isolated from the heavy meromyosin by digestion with papain. This Subfragment 1 appeared as a single peak after chromatography on Sephadex G-200 and DEAE-cellulose. Its migration on disk gel electrophoresis was identical with that of rabbit skeletal Subfragment 1 suggesting a similar molecular ...
G, Bailin, M, Bárány
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Abstract 1. 1.Chicken gizzard Subfragment 1 was isolated from the heavy meromyosin by digestion with papain. This Subfragment 1 appeared as a single peak after chromatography on Sephadex G-200 and DEAE-cellulose. Its migration on disk gel electrophoresis was identical with that of rabbit skeletal Subfragment 1 suggesting a similar molecular ...
G, Bailin, M, Bárány
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European Journal of Biochemistry, 1980
Interaction of actin from chicken gizzard and from rabbit skeletal muscle with rabbit skeletal muscle myosin was compared by measuring the rate of superprecipitation, the activation of the Mg‐ATPase and inhibition of K‐ATPase activity of myosin and heavy meromyosin, and determination of binding of heavy meromyosin in the absence of ATP.
Ewa PRÓCHNIEWICZ +1 more
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Interaction of actin from chicken gizzard and from rabbit skeletal muscle with rabbit skeletal muscle myosin was compared by measuring the rate of superprecipitation, the activation of the Mg‐ATPase and inhibition of K‐ATPase activity of myosin and heavy meromyosin, and determination of binding of heavy meromyosin in the absence of ATP.
Ewa PRÓCHNIEWICZ +1 more
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Studies on the avian gizzard: The development of the gizzard and its innervation
Zeitschrift f�r Zellforschung und Mikroskopische Anatomie, 1969The development of the chick gizzard and its innervation have been studied using histochemical techniques and light and electronmicroscopy. In Hamburger-Hamilton stage 28–29 (6-day old) embryos, the primordium of the gizzard consists of a vascularised mesenchymal thickening of the gut.
T, Bennett, J L, Cobb
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Rapid purification of chicken gizzard α-actinin
Biochemical and Biophysical Research Communications, 1979Abstract A method of purification has been developed which yields highly purified α-actinin and requires less than one day to complete. The α-actinin is extracted from washed chicken gizzard muscle with water at 37°. Actin and a 55,000 dalton protein are quantitatively precipitated from the extract with 20 mM MgCl2.
J E, Niedel, P, Cuatrecasas
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Chicken gizzard, a myoglobin containing smooth muscle
Experientia, 1971In der glatten Muskulatur des Huhnermuskelmagens konnte ein wasserlosliches Hamoprotein nachgewiesen werden, das sich chromatographisch und spektrophotometrisch wie Myoglobin verhalt.
U, Gröschel-Stewart +2 more
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