A Peptide Material from Myosin Containing Sulfhydryl Groups.
نویسندگان
چکیده
منابع مشابه
Actin from Heart Muscle: Sulfhydryl Groups.
• A comparison of a number of chemical features of actin prepared from cardiac and skeletal muscle has been undertaken in an attempt to evaluate the role that this contractile protein may play in determining specific physiological responses by the two types of muscle. Analyses of physicochemical properties 1 and amino acid compositions failed to reveal significant differences between these prot...
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Cyanylation of myosin with 6-thiol’4Clcyanato-9-/3-o-ribofuranosylpurine shows a biphasic effect. During the incorporation of the first 4 mol of cyanide the Mg”+-dependent ATPase activity increases approximately &fold, the Ca*+ activity rises only slightly, and the K+(EDTA) activity falls to approximately 5% of its original value. These enzyme preparations can still be inactivated by N-ethylmal...
متن کاملThiolysis of dinitrophenylated sulfhydryl groups in gizzard myosin. Restoration of regulatory properties in a reconstituted actomyosin.
Dinitrophenylated chicken gizzard myosin which had incorporated 5.2 mol of l-fluoro-2,4-dinitrobenzene/4.7 x 10' g of protein failed to form a calcium-sensitive actomyosin. Thiolysis of 2 mol of the dinitrophenyl group from modified gizzard myosin with 2-mercaptoethanol restored its ability to form a calcium-sensitive actomyosin. It was determined that the dinitrophenyl group was removed from t...
متن کاملSulfhydryl Groups in Proteins
Egg albumin in the native, unaltered state, does not give tests characteristic of sulfhydryl groups. When, however, this protein is treated in any one of several ways, such as by heat (8, 9, 17), ultraviolet irradiation (lo), shaking (lo), or by solution in urea or other amides (7), free sulfhydryl groups make their appearance. The amount of free -SH groups appearing in egg albumin through the ...
متن کاملIsolation of a protein component of sodium-potassium transport adenosine triphosphatase containing ligand-protected sulfhydryl groups.
The sodiumand potassium-activated adenosine triphosphatase (Naf + K+)-ATPase was partially purified from a microsomal fraction of whole rabbit brain, homogenized in a deoxycholate buffer. Suspension and separation by flotation of the resulting lipoproteins in a linear gradient of potassium iodide formed the basis of a rapid preparative technique, whereby the enzyme-containing lipoproteins were ...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1958
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.12-0503