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Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Payne, Deborah A. / Schlattmann, Peter / Tate, Jillian R.

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Rank 5 out of 30 in category Medical Laboratory Technology in the 2014 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2015: 0.873
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Volume 40, Issue 8 (Aug 2002)


An Ideal Substrate for the Measurement of Pancreatic Amylase?

Klaus Lorentz
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/CCLM.2002.134


The advanced knowledge on substrate cleavage by human α-amylases promotes the development of chromogenic maltotriosides exclusively cleaved at the aglycone bond. Three essentials are required for this type of binding at the active site of the enzyme: (i) A minimal hydrophobic modification at the ultimate glucose unit to exclude the condensation of reaction products, (ii) a non-ionic substituent in the 2-position of the phenolic chromophore, and (iii) pertinent effectors to accomodate the aglycone at subsite +1. The novel substrate 2-chloro-4-nitrophenyl-α-D-maltotrioside (acG3-CNP) is presented as an example together with measurement conditions which allow a direct, sensitive and specific measurement of pancreatic amylase without stoichiometric calculations.

About the article

Published Online: 2005-06-01

Published in Print: 2002-08-26

Citation Information: Clinical Chemistry and Laboratory Medicine, ISSN (Print) 1434-6621, DOI: https://doi.org/10.1515/CCLM.2002.134. Export Citation

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