منابع مشابه
Multiple Forms of Acanthamoeba Myosin
Extracts of Acanthamoeba castellanii were previously known to contain two myosin-like ATPases: Acanthumoeba myosin II, a double-headed enzyme of native molecular weight of about 400,000 comprised of two heavy chains of about 170,000 daltons and two pairs of light chains of about 17,500 and 17,000 daltons; and Acanthxwweba myosin I, a single-headed enzyme of native molecular weight of about 180,...
متن کاملAcanthamoeba myosin. I. Isolation from Acanthamoeba castellanii of an enzyme similar to muscle myosin.
An ATPase that accounts for about 0.3% of the total cell protein has been isolated in 90% purity from Acanfhamoeba castellanii. The enzyme has been identsed as a myosinlike ATPase by the following criteria. Maximal enzymatic activity occurs in the presence of EDTA and 0.5 M KCl, and is only 10 to 20% as high in the presence of Ca2+ and less than 1% in the presence of Mg2+. The Mg2+ ATPase is ac...
متن کاملAcanthamoeba Myosin I. ISOLATION FROM ACANTHAMOEBA CAXTELLANII OF AN ENZYME SIMILAR TO MUSCLE MYOSIN*
An ATPase that accounts for about 0.3% of the total cell protein has been isolated in 90% purity from Acanfhamoeba castellanii. The enzyme has been identsed as a myosinlike ATPase by the following criteria. Maximal enzymatic activity occurs in the presence of EDTA and 0.5 M KCl, and is only 10 to 20% as high in the presence of Ca2+ and less than 1% in the presence of Mg2+. The Mg2+ ATPase is ac...
متن کاملGenetic evidence that Acanthamoeba myosin I is a true myosin.
Acanthamoeba castellanii contains two enzymes, myosins IA and IB, that exhibit the catalytic properties of a myosin but possess very unusual physical properties, the most striking of which are their single, low molecular weight heavy chain, their globular shape, and their inability to form bipolar filaments. We have now isolated a putative myosin IB heavy chain gene from Acanthamoeba, using as ...
متن کاملPlasma membrane association of Acanthamoeba myosin I
Myosin I accounted for approximately 2% of the protein of highly purified plasma membranes, which represents about a tenfold enrichment over its concentration in the total cell homogenate. This localization is consistent with immunofluorescence analysis of cells that shows myosin I at or near the plasma membrane as well as diffusely distributed in the cytoplasm with no apparent association with...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43719-8