Determination of LD-Ig complex with counter immunoelectrophoresis using terylene cellulose acetate membrane as

Z J Liu1, X Yang

  • 1Clinical Laboratory, Southwestern Hospital, Chongqing, People's Republic of China.

Insights

A new counter immunoelectrophoresis method effectively identifies abnormal lactate dehydrogenase (LD) isoenzyme bands in serum. This technique, using terylene cellulose acetate, is simple and suitable for routine clinical diagnosis of LD anomalies.

Area of Science:

  • Biochemistry
  • Clinical Chemistry

Background:

  • Lactate dehydrogenase (LD) isoenzymes play crucial roles in cellular metabolism.
  • Identifying abnormal LD isoenzyme bands in serum is important for diagnosing various medical conditions.
  • Existing methods for LD isoenzyme analysis can be complex and time-consuming.

Purpose of the Study:

  • To establish a simple and efficient method for determining abnormal LD isoenzyme bands in serum.
  • To identify LD-Ig complexes using counter immunoelectrophoresis.
  • To evaluate the utility of terylene cellulose acetate as a supporting medium for LD isoenzyme analysis.

Main Methods:

  • Serum samples were analyzed using isoenzyme electrophoresis with a Paragon electrophoretic system.
  • Counter immunoelectrophoresis with terylene cellulose acetate as the supporting medium was employed to identify LD anomalies.
  • The method focused on the identification of the LD-Ig complex.

Main Results:

  • An abnormal LD-4 band was detected in a post-burn patient's serum.
  • An additional band, identified as an LD-IgG complex, was observed on the cathodic side of LD-5.
  • The counter immunoelectrophoresis method proved effective in identifying these abnormal bands.

Conclusions:

  • A useful and efficient protocol combining isoenzyme electrophoresis and counter immunoelectrophoresis was developed.
  • The described counter immunoelectrophoresis method using terylene cellulose acetate is simple and practical.
  • This method is suitable for routine clinical application in identifying abnormal isoenzyme bands.
Abstract