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  • Title: Radioimmunoassay of human salivary amylase: cross-reactivity with human and porcine pancreatic amylase and other salivary proteins.
    Author: Agarwal RP, Henkin RI.
    Journal: Metabolism; 1984 Sep; 33(9):797-807. PubMed ID: 6206375.
    Abstract:
    A radioimmunoassay (RIA) of human salivary amylase was developed. Human salivary and pancreatic amylases were purified by Sephacryl S-200 gel filtration and by cation-exchange chromatography. Human salivary amylase antibody, raised in New Zealand white rabbits, did not crossreact with other salivary proteins and there was also no crossreactivity with purified porcine pancreatic amylase. The antibody crossreacted with human pancreatic amylase to the extent of 25%. Amylase concentrations, estimated by RIA, in human saliva, serum, and urine were compared with enzymatic activity. Correlation of results obtained by the two techniques was best for estimation of amylase in saliva, least for serum and intermediate for urine. Amylase concentrations and enzymatic activity in stimulated parotid saliva were not correlated with flow rate of secretion. There was no correlation between amylase concentrations (and enzymatic activity) in parotid saliva and those found either in serum and urine. Amylase comprises approximately 5% of the total parotid salivary protein in humans.
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