Cerebrospinal fluid enzymology: Creatine kinase, lactate dehydrogenase activity and isozyme pattern as a brain damage index

1978 ◽  
Vol 89 (3) ◽  
pp. 405-409 ◽  
Author(s):  
J.L. Viallard ◽  
J. Gaulme ◽  
B. Dalens ◽  
B. Dastugue
1984 ◽  
Vol 30 (10) ◽  
pp. 1708-1709
Author(s):  
D L Smalley ◽  
B Womack ◽  
C Handorf ◽  
S Acchiardo

Abstract A 65-year-old woman failed to develop increased creatine kinase or lactate dehydrogenase activity after a myocardial infarction. She had no measurable creatine kinase MB isoenzyme and no detectable patterns of normal LD isoenzyme activity. These determinations five months after the infarction showed normal values for total activity and isoenzyme patterns.


1976 ◽  
Vol 22 (8) ◽  
pp. 1405-1407 ◽  
Author(s):  
P M Bayer ◽  
F Gabl ◽  
G Granditsch ◽  
K Widhalm ◽  
H Zyman ◽  
...  

Abstract We present a case of a 11/2-year-old boy with toxic enteritis, consecutive consumption coagulopathy, and sever brain damage. During the acute phase we found high activity of the BB isoenzyme of creatine kinase in cerebrospinal fluid, but not in the serum. Isoenzyme MM could also be found in the spinal fluid (37.9% of the total activity). We conclude that analysis for creatine kinase isoenzymes in spinal fluid is of clinical importance.


1986 ◽  
Vol 32 (10) ◽  
pp. 1901-1905 ◽  
Author(s):  
J C Koedam ◽  
G M Steentjes ◽  
S Buitenhuis ◽  
E Schmidt ◽  
R Klauke

Abstract We produced three batches of a human-serum-based enzyme reference material (ERM) enriched with human aspartate aminotransferase (EC 2.6.1.1), alanine aminotransferase (EC 2.6.1.2), creatine kinase (EC 2.7.3.2), and lactate dehydrogenase (EC 1.1.1.27). The added enzymes were not exhaustively purified; thus the final ERMs contained some enzymes as contaminants, of which only glutamate dehydrogenase activity might interfere. The stability during storage and after reconstitution was good. The commutability of the four enzymes in the three ERM batches was also good, except when German or Scandinavian methods for aminotransferases were involved. The temperature-conversion factors for the ERMs were equivalent to those for patients' sera. Reactivation after reconstitution was complete within 5 min and was independent of the temperature of the reconstitution fluid. We believe that these secondary ERMs will aid in the transfer of accuracy between well-defined reference methods and daily working methods so that clinical enzymology results will become more comparable from laboratory to laboratory.


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