Clinical Chemistry Link to Randox Laboratories Web Site
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 23: 229-233, 1977;
This Article
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gershbein, L. L.
Right arrow Articles by Raikoff, K. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gershbein, L. L.
Right arrow Articles by Raikoff, K. G.

Clinical Chemistry, Vol 23, 229-233, Copyright © 1977 by American Association for Clinical Chemistry

Total lactate dehydrogenase and its isoenzymes in serum in the presence of penicillamine and other sulfhydryl compounds

LL Gershbein and KG Raikoff

Toward delineation of changes in total lactate dehydrogenase (LDH) and in the distribution of LDH isoenzymes as assessed by polyacrylamide disc electrophoresis, we inbucated human and rat sera with various agents, notably sulfhydryl compounds. Although artefacts were apparent when these agents were used without preliminary adjustment of pH, we saw little alteration in total unitage when one or two volumes of serum was mixed with one volume of any of several thiols, especially penicillamine, at an initial concentration of 0.4 mol/liter and pH 7.0- 7.5. Under these conditions, penicillamine caused a loss in LDH-5 after incubation for 1 h at 25 degrees C together with small decreases in mobility of the other four isoenzymes toward the anode. A zymosan region appeared below the albumin and tracking dye area. With longer periods of incubation of rat serum with penicillamine or alpha- mercaptosuccinate, a novel band in the zymogram was noted just above the LDH-4 peak. The observations are discussed in terms of allosteric effectors.


The following articles in journals at HighWire Press have cited this article:


Home page
 Annals of Clinical & Laboratory ScienceHome page
K. Fujita, H. Sato, F. Kameko, F. Terasawa, N. Okumura, M. Sugano, K. Yamauchi, M. Maekawa, and I. Sakurabayashi
An Immunoglobulin A1 that Inhibits Lactate Dehydrogenase Activity, with Reversal of Inhibition by Addition of NADH
Ann. Clin. Lab. Sci., January 1, 2006; 36(4): 461 - 468.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1977 by the American Association for Clinical Chemistry.