Korean J Lab Med.  2003 Aug;23(4):242-245.

Alteration of Lactate Dehydrogenase Isoenzyme Pattern Observed from CSF in Patients with Meningitis by Streptococcus pneumoniae

• Shin KS
• Son BR

Abstract

The bacterial protein streptokinase binds to LD-M subunits, which shares a small region of homology with the site on plasminogen to which streptokinase is known to bind. We found an extra band of LD activity in CSF in a patient, suffering from meningitis due to Streptococcus pneumoniae. We performed a LD isoenzyme electrophoresis of the serum mixed with supernates from cultured broth of several species of streptococci. To investigate the effect on serum LD activity, we analyzed LD activity after the mixing of the serum with products of S. pneumoniae. S. pneumoniae, groups A and C beta hemolytic streptococci, revealed the extra band of LD activity at the origin site. The supernates of cultured broth of S. pneumoniae inhibited LD activity of the serum. Streptokinase or streptokinase-like substances can form complexes with LD in vivo after streptococcal infection, with consequent alteration of the LD isoenzyme pattern.

Keyword

LD isoenzyme; Streptokinase; Streptococcus pneumoniae; Extra band

MeSH Terms

Bacterial Proteins
Electrophoresis
Humans
L-Lactate Dehydrogenase*
Meningitis*
Plasminogen
Pneumonia
Streptococcal Infections
Streptococcus pneumoniae*
Streptokinase
Bacterial Proteins
L-Lactate Dehydrogenase
Plasminogen
Streptokinase