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Clinical Chemistry 43: 2318-2322, 1997;
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(Clinical Chemistry. 1997;43:2318-2322.)
© 1997 American Association for Clinical Chemistry, Inc.


Articles

Secretory carbonic anhydrase isoenzyme (CA VI) in human serum

Jyrki Kivelä1,2,a, Seppo Parkkila1,3, Abdul Waheed3, Anna-Kaisa Parkkila1,3, William S. Sly3 and Hannu Rajaniemi1

1 Department of Anatomy, University of Oulu, Oulu, Finland.

2 Parolannummi Garrison Hospital, Finnish Defence Forces, Hattula, Finland.

3 Edward A. Doisy Department of Biochemistry and Molecular Biology, St. Louis University School of Medicine, St. Louis, MO.
a Address correspondence to this author at: Parolannummi Garrison Hospital, P.O. Box 5, FIN-13701 Parolannummi, Finland. Fax 358–3-1814–4612; e-mail jyrki.kivela{at}pp.inet.fi

Carbonic anhydrase VI (CA VI) is a secretory isoenzyme that, by analogy to {alpha}-amylase, is produced in the salivary glands and delivered into saliva. To determine whether CA VI is transferred into the circulation and is detectable in human serum, we collected blood samples from four healthy subjects at 3-h intervals throughout a 24-h period and measured concentrations of CA VI by a specific time-resolved immunofluorometric assay. All serum samples contained CA VI, the concentrations being ~22 times lower in serum than in the corresponding saliva samples. The presence of CA VI in serum was confirmed by Western blotting, which under reducing conditions identified a 42-kDa polypeptide band corresponding to the monomeric CA VI. The described time-resolved immunofluorometric assay for CA VI might be useful to identify or exclude diseases of the salivary glands in the differential diagnosis of patients whose serum amylase concentrations are increased.




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


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Proc. Natl. Acad. Sci. USAHome page
P. Karhumaa, J. Leinonen, S. Parkkila, K. Kaunisto, J. Tapanainen, and H. Rajaniemi
The identification of secreted carbonic anhydrase VI as a constitutive glycoprotein of human and rat milk
PNAS, September 5, 2001; (2001) 121172598.
[Abstract] [Full Text] [PDF]


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J. Physiol.Home page
J. Kivela, S. Parkkila, A.-K. Parkkila, J. Leinonen, and H. Rajaniemi
Salivary carbonic anhydrase isoenzyme VI
J. Physiol., October 15, 1999; 520(2): 315 - 320.
[Abstract] [Full Text] [PDF]


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J. Histochem. Cytochem.Home page
J. Saarnio, S. Parkkila, A.-K. Parkkila, A. Waheed, T. Karttunen, and W. S. Sly
Cell-specific Expression of Mitochondrial Carbonic Anhydrase in the Human and Rat Gastrointestinal Tract
J. Histochem. Cytochem., April 1, 1999; 47(4): 517 - 524.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
P. Karhumaa, J. Leinonen, S. Parkkila, K. Kaunisto, J. Tapanainen, and H. Rajaniemi
The identification of secreted carbonic anhydrase VI as a constitutive glycoprotein of human and rat milk
PNAS, September 25, 2001; 98(20): 11604 - 11608.
[Abstract] [Full Text] [PDF]




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Copyright © 1997 by the American Association for Clinical Chemistry.