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 13 February 1970:
Vol. 167. no. 3920, pp. 994 - 996
DOI: 10.1126/science.167.3920.994

Articles

Horseshoe Crab Lactate Dehydrogenase: Tissue Distribution and Molecular Weight

Edward J. Massaro 1

1 Department of Biochemistry, State University of New York at Buffalo, Buffalo 14214

Lactate dehydrogenase from Xiphosura (Limulus) polyphemus i D(-)-lactate specific. It does not use L(+)-lactate, agr-hydroxybutyrate, agr-hydroxyvalerate, or agr-hydroxyisocaproate as substrate. In most tissues lactate dehydrogenase is composed of five isozymes with a molecular weight of 140,000 for each, as judged by gel-filtration chromatography. This suggests that the isozyme, are tetramers comprised of varying amounts of two physicochemically distinc subunits.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Horseshoe Crab Lactate Dehydrogenases: Evidence for Dimeric Structure.
R. K. Selander and S. Y. Yang (1970)
Science 169, 179-181
   Abstract »    PDF »



To Advertise     Find Products


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