Isolation and Characterization of a Lysolecithin-Adenosine Triphosphatase Complex from Lobster Muscle Microsomes
نویسندگان
چکیده
منابع مشابه
Salt-stimulated Adenosine Triphosphatase from Smooth Microsomes of Turnip.
The turnip (Brassica rapa L.) microsome fraction contains both a Mg(2+)-inhibited acid phosphatase and a salt-stimulated Mg(2+)-activated ATPase. However, as the pH optimum of the ATPase was 8.0 to 8.5, the acid phosphatase activity could be eliminated by assaying at or above pH 7.8. The ATPase was concentrated in a fraction equivalent to the smooth microsomal membranes and was not due to fragm...
متن کاملAdenosine triphosphatase activities of muscle sarcolemma.
Isolated sarcolemma hydrolyzed ATP in the presence of Mg2+ and Ca2+. MgATPase was stimulated by low concentrations of Ca2+ and inhibited by high concentrations of this cation. Membranes hydrolyzed p-nitrophenylphosphate in the presence of Mg 2+; this activity was stimulated by Ca2f and K+. La3f stimulated MgATPase at low concentrations (up to 50 pM) and caused inhibition at higher concentration...
متن کاملIsolation and characterization of coronary endothelial and smooth muscle cells from A1 adenosine receptor-knockout mice.
Mice have been used widely in in vivo and in vitro cardiovascular research. The availability of knockout mice provides further clues to the physiological significance of specific receptor subtypes. Adenosine A(1) receptor (A(1)AR)-knockout (A(1)KO) mice and their wild-type (A(1)WT) controls were employed in this investigation. The heart and aortic arch were carefully removed and retroinfused wi...
متن کاملIsolation of oligomycin-sensitive adenosine triphosphatase from beef heart mitochondria and analysis of its fine structure.
1. An oligomycin -sensitive ATPase was isolated and partially purified from beef heart mitochondria. The specific activity of ATPase sensitive to oligomycin of the fraction was five to eight times that of aged mitochondrial or of DNP-induced mitochondrial ATPase assayed under the same condition. 2. Electron micrographs of the partially purified oligomycinsensitive ATPase reveal a structure in w...
متن کاملPurification and Characterization of a Cation-stimulated Adenosine Triphosphatase from Corn Roots.
A membrane-bound, monovalent cation-stimulated ATPase from Zea mays roots has been purified to a single band on sodium dodecyl sulfate gel electrophoresis. Microsomal preparations with K(+) -stimulated ATPase activity were extracted with 1 m NaClO(4), and the solubilized enzyme was purified by chromatography on columns of n-hexyl-Sepharose, DEAE-cellulose, and Sephadex G-100 Superfine. A 500-fo...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43628-4