Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 25 August 1967:
Vol. 157. no. 3791, pp. 945 - 946
DOI: 10.1126/science.157.3791.945
Prev | Table of Contents | Next

Articles

Ultrastructure of Thrombosthenin, the Contractile Protein of Human Blood Platelets

Dorothea Zucker-Franklin 1, Ralph L. Nachman 2, and Aaron J. Marcus 3

1 New York University School of Medicine, New York
2 New York Hospital, Cornell Medical Center, Ithaca
3 New York Veterans Administration Hospital, New York

Partially purified thrombosthenin with adenosine triphosphatase activity similar to that of actomyosin was subjected to electron microscopy. More than 50 percent of the material consisted of fibrils 80 to 100 angstroms in width. Occasional fibrils suggested a periodic structure. The morphology of isolated thrombosthenin resembled that of microfibrils in the cytoplasm and pseudopods of intact platelets.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Microfilaments in Cellular and Developmental Processes.
N. K. Wessells, B. S. Spooner, J. F. Ash, M. O. Bradley, M. A. Luduena, E. L. Taylor, J. T. Wrenn, and K. M. Yamada (1971)
Science 171, 135-143
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)