Clinical Chemistry
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Clinical Chemistry 25: 461-465, 1979;
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Urdal, P.
Right arrow Articles by Landaas, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Urdal, P.
Right arrow Articles by Landaas, S.

Clinical Chemistry, Vol 25, 461-465, Copyright © 1979 by American Association for Clinical Chemistry

Macro creatine kinase BB in serum, and some data on its prevalence

P Urdal and S Landaas

We report the case of a patient with persistently above-normal activity of creatine kinase (CK) in serum, a major fraction of which on electrophoresis moved as a band between the MM and MB isoenzymes and on anion-exchange column chromatography eluted in the MB fraction. Measurements in the presence of specific M or B subunit-inhibitory antibodies indicated that 93% of the activity consisted of B-isomers. From these experiments we conclude that the abnormal CK is of BB nature. Gel filtration and immunoglobulin precipitation showed that the CK-BB was complexed with IgG. Normal CK-BB, when mixed with the patient's serum, was converted to macro CK-BB. In vitro stability of 37 degrees C of the abnormal enzyme was much greater than that of normal BB and MM isoenzymes. Following this finding, we then assessed 310 sera, received for enzyme assay by the clinical laboratory, for electrophoretically abnormally migrating CK isoenzymes. Of these, five (1.6%) contained such enzymes, all being of BB nature. They were of increased molecular mass, and at least three of them were complexed with IgG.


The following articles in journals at HighWire Press have cited this article:


Home page
 CMAJHome page
L. Babuin and A. S. Jaffe
Troponin: the biomarker of choice for the detection of cardiac injury
Can. Med. Assoc. J., November 8, 2005; 173(10): 1191 - 1202.
[Abstract] [Full Text] [PDF]

Home page
 Clin. Chem.Home page
R. Rej
Clinical Chemistry through Clinical Chemistry: A Journal Timeline
Clin. Chem., December 1, 2004; 50(12): 2415 - 2458.
[Abstract] [Full Text] [PDF]

Home page
 Arch Intern MedHome page
T. H. Lee, M. C. Weisberg, E. F. Cook, K. Daley, D. A. Brand, and L. Goldman
Evaluation of Creatine Kinase and Creatine Kinase--MB for Diagnosing Myocardial Infarction: Clinical Impact in the Emergency Room
Arch Intern Med, January 1, 1987; 147(1): 115 - 121.
[Abstract] [PDF]

Home page
 ANN INTERN MEDHome page
T. H. LEE and L. GOLDMAN
Serum Enzyme Assays in the Diagnosis of Acute Myocardial InfarctionRecommendations Based on a Quantitative Analysis
Ann Intern Med, August 1, 1986; 105(2): 221 - 233.
[Abstract] [PDF]

Home page
 JAMAHome page
C. J. Bark
Mitochondrial Creatine Kinase: A Poor Prognostic Sign
JAMA, May 23, 1980; 243(20): 2058 - 2060.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1979 by the American Association for Clinical Chemistry.