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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 3583-18144612; e-mail jyrki.kivela{at}pp.inet.fi
Carbonic anhydrase VI (CA VI) is a secretory isoenzyme that, by analogy
to
-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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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. 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. 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] |
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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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