A myosin-like protein from smooth muscle.

نویسندگان

  • K Kohama
  • Y Lin
  • H Takano-Ohmuro
  • R Ishikawa
چکیده

A protein was purified from chicken gizzard smooth muscle. It bound ATP and actin. Actin activated the Mg2(+)-ATPase activity of this protein. The Ca2(+)-ATPase activity was lower than K(+)-EDTA ATPase activity. Thus, it appears that this protein is akin to myosin I rather than to conventional myosin. However, ATPase activities of the protein were much lower than those of myosin I. A protein cofactor, such as protein kinase, which would enhance these activities remains to be purified from the smooth muscle.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Smitin, a novel smooth muscle titin–like protein, interacts with myosin filaments in vivo and in vitro

Smooth muscle cells use an actin-myosin II-based contractile apparatus to produce force for a variety of physiological functions, including blood pressure regulation and gut peristalsis. The organization of the smooth muscle contractile apparatus resembles that of striated skeletal and cardiac muscle, but remains much more poorly understood. We have found that avian vascular and visceral smooth...

متن کامل

Stimulation of the interaction between actin and myosin by Physarum caldesmon-like protein and smooth muscle caldesmon.

We have purified an actin-binding protein from the plasmodia of a lower eukaryote, Physarum polycephalum, with an apparent molecular mass of 210,000 daltons on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This protein bound to actin filaments with a stoichiometry of 1:7-8 in a Ca(2+)-calmodulin-dependent manner. Antibody raised against caldesmon from smooth muscle cross-reacted wi...

متن کامل

Detection and ultrastructural localization of human smooth muscle myosin-like molecules in human non-muscle cells by specific antibodies.

Spectrin, a protein complex which is peripherally attached to the cytoplasmic surface of the human erythrocyte membrane, cannot be detected (by complement fixation with anti-spectrin antibodies) in homogenates of several different human non-muscle cells studied. On the other hand, a protein antigenically identical or similar to human smooth muscle myosin was detected (by complement fixation wit...

متن کامل

Proteomic analysis of muscle tissue from rainbow trout (Oncorhynchus mykiss) fed dietary β-glucan

The aim of this study was to examine the changes in muscle proteome of the rainbow trout fed dietary β-glucan. The experimental diets contained 0 (control), 0.1% and 0.2% β-1,3/1,6 yeast glucan. First, feeding larvae were fed to apparent satiation nine times per day with their respective diets over two months. The percentage of body weight gain and feed efficiency of fish fed 0.2% diet was sign...

متن کامل

Moyamoya-like cerebrovascular disease in a child with a novel mutation in myosin heavy chain 11

Heterozygous mutations in theMYH11 gene affecting the C-terminal coiled-coil region of the smooth muscle myosin heavy chain, a contractile protein of smooth muscle cells (SMC), have been described to cause thoracic aortic aneurysm or aortic dissection (TAAD) and patent ductus arteriosus (PDA). Herein we expand the phenotype associated withMYH11mutations to include moyamoya-like cerebrovascular ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Journal of cell science. Supplement

دوره 14  شماره 

صفحات  -

تاریخ انتشار 1991