635th MEETING, ABERDEEN 1287 potential. Now that differences in expression of specific cellsurface oligosaccharides have been identified, it is necessary to analyse the protein components of the intact molecules in order t o determine whether the observed changes are modulated by identical groups of glycoproteins in the different metastatic phenotypes.We are grateful to Coulter Electronics Ltd, U.K. for theii invaluahle advice and assistance with this project.
Six different methods for alpha-amylase determination were compared by assaying human serum samples covering a wide range of alpha-amylase values. All the methods studied use as substrate a maltooligosaccharide with a chromophore group at the reducing end; some are chemically blocked at the nonreducing end. Intermethod comparison by regression and correspondence analyses showed significant differences for two methods. The commutability of 12 commercial control materials containing alpha-amylase was also assessed by the different methods in comparison with human serum specimens containing the pancreatic and salivary isoenzymes. We also studied the behavior of pancreatic and salivary materials prepared in our laboratory. Control materials with alpha-amylase of non-human origin were not commutable with the enzyme in human sera and should not be used for intermethod calibration.
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