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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.
R P Agarwal, and
R I Henkin
April 1978,
Analytical biochemistry,
R P Agarwal, and
R I Henkin
January 1981,
Methods in enzymology,
R P Agarwal, and
R I Henkin
September 1989,
Annals of clinical biochemistry,
R P Agarwal, and
R I Henkin
October 1979,
Clinica chimica acta; international journal of clinical chemistry,
R P Agarwal, and
R I Henkin
September 1980,
Research communications in chemical pathology and pharmacology,
R P Agarwal, and
R I Henkin
May 1974,
Biochimica et biophysica acta,
R P Agarwal, and
R I Henkin
February 1970,
Archives of biochemistry and biophysics,
R P Agarwal, and
R I Henkin
January 1987,
Gene,
R P Agarwal, and
R I Henkin
April 1985,
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
R P Agarwal, and
R I Henkin
April 1978,
The Journal of laboratory and clinical medicine,
