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 31 July 1970:
Vol. 169. no. 3944, pp. 480 - 481
DOI: 10.1126/science.169.3944.480
Prev | Table of Contents | Next

Articles

Lactate Dehydrogenase Isozymes: Further Kinetic Studies at High Enzyme Concentration

Thomas Wuntch 1, Raymond F. Chen 1, and Elliot S. Vesell 1

1 Milton S. Hershey Medical Center, Pennsylvania State University College of Medicine, Hershey 17033 and National Heart and Lung Institute, Bethesda, Maryland 20014

By competition with lactate dehydrogenase (LDH) for nicotinamide adenine dinucleotide (NAD), commonly occurring intracellular proteins, such as glyceraldehyde-3-phosphate dehydrogenase, malate dehydrogenase, and albumin, can protect LDH-1 and LDH-5 from inhibition and ternary complex formation with NAD and pyruvate. The existence of intracellular proteins that compete with LDH for NAD renders unphysiological a model for estimating the extent of intracellular LDH inhibition based on incubations of only LDH, NAD, and pyruvate.

To Advertise     Find Products

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