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


     

Clinical Chemistry 23: 1853-1856, 1977;
This Article
Right arrow Full Text (PDF)
Right arrow Submit an electronic Letter to
the Editor about this paper
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
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 O'Farrell, H. K.
Right arrow Articles by Brown, H. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O'Farrell, H. K.
Right arrow Articles by Brown, H. D.

Clinical Chemistry, Vol 23, 1853-1856, Copyright © 1977 by American Association for Clinical Chemistry

Calorimetry of cholinesterase activity in serum

HK O'Farrell, SK Chattopadhyay and HD Brown

Cholinesterase activity in human serum was measured calorimetrically and compared to values obtained with the spectrophotometric method of Rappaport et al. [Clin. Chim. Acta 4, 227 (1959)]. The response of the calorimeter upon mixing serum with acetylcholine corresponded to the cholinesterase activity of the serum, the thermogram peak height being linearly related to enzyme activity at serum dilution volumes at which interference heat was negligible. The interference heat contributed by the dilution mixing characteristics of serum, studied separately, was found to be similar for heat-denatured, aged, or lyophilized samples. In all cases, heat of mixing was negligible when 1 ml of serum in buffer (2/3 by vol) was mixed with 1 ml of buffer. When this amount of serum was assayed with acetylcholine, cholinesterase activities of 2 and 3 kU/liter were recorded as thermograms with peak heights of 2.3 and 3.5 cm, respectively.


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


Home page
 J. Biol. Chem.Home page
P. A. Pioli, B. J. Hamilton, J. E. Connolly, G. Brewer, and W. F. C. Rigby
Lactate Dehydrogenase Is an AU-rich Element-binding Protein That Directly Interacts with AUF1
J. Biol. Chem., September 13, 2002; 277(38): 35738 - 35745.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1977 by the American Association for Clinical Chemistry.