scholarly journals Evaluation of Stress on Menstrual Cycle Using Salivary Amylase Activity

2012 ◽  
Vol 24 (3) ◽  
pp. 123-127
Author(s):  
Asami Nakagawa ◽  
Makoto Sasaki ◽  
Masaki Yamaguchi
1985 ◽  
Vol 31 (8) ◽  
pp. 1283-1286 ◽  
Author(s):  
T E Mifflin ◽  
D C Benjamin ◽  
D E Bruns

Abstract In this rapid quantitative assay for pancreatic alpha-amylase (EC 3.2.1.1) in serum, we precipitate salivary amylases by 10-min incubation with monoclonal anti-salivary amylase antibody immobilized on particles of polyvinylidene fluoride. We then centrifuge the serum mixture and measure the pancreatic amylase activity remaining in the supernate by a kinetic method. The assay requires 50 microL of serum and the standard curve is linear to at least 1300 U of pancreatic amylase per liter of serum. CVs were 1.3% within-run, 6-8% day-to-day. Apparent analytical recovery of pancreatic amylase activity added to serum was 101% +/- 2%. Addition of purified salivary amylase, 356 U/L, to sera gave a value for apparent pancreatic amylase of less than 4 U/L, or 1% of the added salivary amylase activity. This assay correlated well with an electrophoretic method (slope, 0.97-0.99; intercept, 0.5 to -4 U/L; correlation coefficient, 0.946-0.990; and standard error of the estimate 3-5 U/L). Estimated normal reference intervals with maltotetraose as substrate were: total amylase, 39-118 U/L; pancreatic amylase, 11-50 U/L; and salivary amylase, 18-79 U/L.


1972 ◽  
Vol 17 (10) ◽  
pp. 1415-1420 ◽  
Author(s):  
B. Wesley-Hadzija ◽  
H. Pigon

1971 ◽  
Vol 17 (4) ◽  
pp. 311-315 ◽  
Author(s):  
Sylvan M Sax ◽  
Anna B Bridgwater ◽  
John J Moore

Abstract We describe a sensitive, precise assay of serum or urine amylase activity, with use of a new substrate, Procion Brilliant Red M-2BS—Amylopectin. After 0.2 ml of serum or urine is incubated with substrate for 10 min at 37°C, ethylene glycol monomethyl ether is added to precipitate proteins and larger substrate particles. Clarity and chromogenicity of the final solution are not sensitive to small changes in temperature or concentrations of the various reagents. No interferences necessitating preparation of specimen blanks have been encountered. Human salivary amylase, assayed by a reference saccharogenic method, is used for calibration. When read against the resulting curve, normal sera and urines give activities comparable to those obtained with the reference method. Human pancreatic extract, sera and urines from pancreatitis patients, and macroamylasemia serum show higher activities by the proposed method.


Author(s):  
Yui Matsuo ◽  
Koji Murai ◽  
Keiichi Fukushi ◽  
Yuji Hayashi ◽  
Laurie C. Stone ◽  
...  

1985 ◽  
Vol 31 (8) ◽  
pp. 1331-1334 ◽  
Author(s):  
M Gerber ◽  
K Naujoks ◽  
H Lenz ◽  
W Gerhardt ◽  
K Wulff

Abstract A monoclonal antibody (66C7) was prepared that specifically binds human salivary amylase (EC 3.2.1.1); it cross reacts with human pancreatic amylase by less than 1%. Two procedures are described for determination of isoamylases in human serum with this antibody: an enzyme immunoassay for determining amylase of salivary origin, and a routine method in which this amylase is immunoprecipitated and the remaining (pancreatic) amylase activity is assayed. Results by the two methods correlate well.


1998 ◽  
Vol 78 (3) ◽  
pp. 279-284 ◽  
Author(s):  
Pao-Li Wang ◽  
Shinya Shirasu ◽  
Mitsuko Shinohara ◽  
Noboru Murakawa ◽  
Masaki Endo ◽  
...  

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