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


     

Clinical Chemistry 31: 14-19, 1985;
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
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 Rauscher, E.
Right arrow Articles by Wahlefeld, A. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rauscher, E.
Right arrow Articles by Wahlefeld, A. W.

Clinical Chemistry, Vol 31, 14-19, Copyright © 1985 by American Association for Clinical Chemistry

Optimized conditions for determining activity concentration of alpha- amylase in serum, with 1,4-alpha-D-4-nitrophenylmaltoheptaoside as substrate

E Rauscher, U Neumann, E Schaich, S von Bulow and AW Wahlefeld

We describe a method for measuring the catalytic activity of alpha- amylase (EC 3.2.1.1) in serum and urine, by use of a defined substrate: 1,4-alpha, D-4-nitrophenyl maltoheptaoside. We use a phosphate buffer of pH 7.10, containing chloride as activator and alpha-glucosidase (EC 3.2.1.20) as the auxiliary enzyme. After a lag phase of 4 min at 25 degrees C or 30 degrees C, or 3 min at 37 degrees C, the increase of absorption of 4-nitrophenol is measured at 410 nm or 405 nm. The pH value of the assay mixture is a compromise between optimum pH for the alpha-amylase reaction, shortest possible lag phase, and an acceptable absorptivity of 4-nitrophenol. Because the dissociation of 4- nitrophenol depends strongly on pH and temperature, we determined its absorptivity with various combinations of these variables in the assay. Heparin-treated plasma can be used, but not EDTA, fluoride, or citrate. Lipemia, hemoglobin less than or equal to mumol/L, bilirubin less than or equal to 170 mumol/L, glucose less than or equal to 100 mmol/L, and ascorbic acid less than or equal to 1 mmol/L of sample do not interfere in the assay.


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


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
M. E. Sabbatini, M. Rodriguez, M. B. di Carlo, C. A. Davio, M. S. Vatta, and L. G. Bianciotti
C-type natriuretic peptide enhances amylase release through NPR-C receptors in the exocrine pancreas
Am J Physiol Gastrointest Liver Physiol, November 1, 2007; 293(5): G987 - G994.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
M. H. Rivera, A. Lopez-Munguia, X. Soberon, and G. Saab-Rincon
{alpha}-Amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity
Protein Eng. Des. Sel., July 1, 2003; 16(7): 505 - 514.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Feller, S. D'Amico, A. M. Benotmane, F. Joly, J. Van Beeumen, and C. Gerday
Characterization of the C-terminal Propeptide Involved in Bacterial Wall Spanning of alpha -Amylase from the Psychrophile Alteromonas haloplanctis
J. Biol. Chem., May 15, 1998; 273(20): 12109 - 12115.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Feller, O. l. Bussy, C. Houssier, and C. Gerday
Structural and Functional Aspects of Chloride Binding to Alteromonas haloplanctis alpha -Amylase
J. Biol. Chem., September 27, 1996; 271(39): 23836 - 23841.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1985 by the American Association for Clinical Chemistry.