Multiple forms of Acanthamoeba myosin I.
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چکیده
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 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...
متن کاملDifferential localization of Acanthamoeba myosin I isoforms
Acanthamoeba myosins IA and IB were localized by immunofluorescence and immunoelectron microscopy in vegetative and phagocytosing cells and the total cell contents of myosins IA, IB, and IC were quantified by immunoprecipitation. The quantitative distributions of the three myosin I isoforms were then calculated from these data and the previously determined localization of myosin IC. Myosin IA o...
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 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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50807-3