Mechanism of protection and activation of creatine kinase isoenzymes by dithiothreitol in human serum.

1977 ◽  
Vol 23 (10) ◽  
pp. 1948-1949
Author(s):  
P S Rao ◽  
R G Evans ◽  
H S Mueller
1978 ◽  
Vol 24 (3) ◽  
pp. 422-428 ◽  
Author(s):  
M H Zweig ◽  
A C Van Steirteghem ◽  
A N Schechter

Abstract We describe a sensitive, specific radioimmunoassay for the BB isoenzyme of creatine kinase (CK-BB) in serum. A sequential saturation assay was used to achieve sufficient sensitivity to detect the isoenzyme in 100-microliter serum samples of all healthy persons and patients tested. Bound and free antigen were separated by a second antibody system. Large excesses of purified isoenzyme MM did not react in the assay. Cross reactivity of two preparations of CK-MB was only 1 to 7+. The 95th percentile of serum CK-BB in 208 healthy adults was 6.2 microgram/liter. Within-assay and between-assay precision ranged from 5.5 to 11.9% and 9.7 to 13.6%, respectively.


1984 ◽  
Vol 44 (7) ◽  
pp. 611-615 ◽  
Author(s):  
Christer Sylvén ◽  
Eva Jansson ◽  
Anders Kallner ◽  
Kim Böök

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.


1992 ◽  
Vol 9 (05/06) ◽  
pp. 456-459 ◽  
Author(s):  
Andrew Satin ◽  
Gary Hankins ◽  
Wayne Patterson ◽  
Richard Scott

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