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.

Science 8 November 1968:
Vol. 162. no. 3854, pp. 685 - 686
DOI: 10.1126/science.162.3854.685
Prev | Table of Contents | Next

Articles

D-Lactate Specific Pyridine Nucleotide Lactate Dehydrogenase in Animals

George L. Long 1 and Nathan O. Kaplan 1

1 Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02154

A survey of representative invertebrates has revealed the presence of pyridine nucleotide-linked D-lactate dehydrogenase in a number of groups. All species studied contained either DD-or LL-lactate dehydrogenase, but no species contained both enzymes. The D-lactate dehydrogenase from Limulus polyphemus has been purified and has a molecular weight of 65,000.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation.
C. Markert, J. Shaklee, and G. Whitt (1975)
Science 189, 102-114
   PDF »
Horseshoe Crab Lactate Dehydrogenases: Evidence for Dimeric Structure.
R. K. Selander and S. Y. Yang (1970)
Science 169, 179-181
   Abstract »    PDF »
Horseshoe Crab Lactate Dehydrogenase: Tissue Distribution and Molecular Weight.
E. J. Massaro (1970)
Science 167, 994-996
   Abstract »    PDF »


To Advertise     Find Products

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