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Lactate dehydrogenase isoenzyme composition of human platelets
D S Miyada1, A Fagin, H Pirkle
1Department of Pathology, University of California, Irvine Medical Center, Orange 92668.
Clinical Chemistry
|December 1, 1989
Summary
Platelet preparations show consistent lactate dehydrogenase (LDH) isoenzyme ranking but differing percentages compared to prior studies. Freezing and thawing releases LDH similarly to homogenization.
Area of Science:
- Biochemistry
- Hematology
- Clinical Chemistry
Background:
- Lactate dehydrogenase (LDH) is an enzyme crucial in cellular metabolism.
- LDH exists in various isoenzyme forms, reflecting tissue-specific expression.
- Understanding platelet LDH isoenzyme composition is vital for interpreting clinical findings.
Purpose of the Study:
- To determine the isoenzyme composition of platelet preparations.
- To compare these findings with existing literature.
- To investigate LDH release mechanisms in platelets.
Main Methods:
- Electrophoresis was used to analyze LDH isoenzymes in 12 platelet preparations.
- Statistical analysis was performed to determine mean percentages and standard deviations.
- Platelet LDH release was compared between freezing/thawing and homogenization methods.
Main Results:
- The mean percentages of LDH isoenzymes were LDH-1 (16.6%), LDH-2 (30.1%), LDH-3 (34.2%), LDH-4 (18.2%), and LDH-5 (0.9%).
- The isoenzyme ranking was consistent with previous data, but percentages, especially for LDH-1 and LDH-4, differed significantly.
- LDH release was comparable whether platelets were subjected to freezing/thawing or homogenization.
Conclusions:
- Platelet LDH isoenzyme profiles exhibit a consistent prevalence ranking.
- Significant variations in LDH isoenzyme percentages exist compared to prior reports.
- Platelet LDH is readily released through common laboratory procedures like freezing/thawing and homogenization.