SomogyiM.Micromethods for the estimation of diastase. J Biol Chem1938; 125: 399–414.
2.
FooAYRosalkiSB. Measurement of plasma amylase activity. Ann Clin Biochem1986; 23: 624–37.
3.
Kruse-JarresJDKaiserC.Evaluation of a new α-amylase assay using 4,6-ethylidene-(G7)-1,4-nitrophenyl-(G1)-α-D-maltoheptaoside as substrate. J Clin Chem Clin Biochem1989; 27: 103–13.
4.
DupuyGHilaireGAubryC.Rapid determination of α-amylase activity by the use of a new chromogenic substrate. Clin Chem1987; 33: 524–8.
5.
ElbinCSBecksSLeppCA. Evaluation of silyl-blocked p-nitrophenylmaltoheptaoside as a substrate for α-amylase reagents. Clin Chem1993; 39: 112–18.
6.
OgawaZMatsubayashiYSatohSOritaNItohH.Isopropylidine maltoheptaosyl fructofuranoside, doubly blocked substrate for determination of endoamylase activity. Clin Chem1991; 37: 1323–8.
7.
TietzNW. Amylase measurements in serum—old myths die hard [Editorial]. J Clin Chem Clin Biochem1988; 26: 251–3.
8.
RobytDFFrenchD.The action pattern of porcine pancreatic α amylase in relationship to the substrate binding site of the enzyme. J Biol Chem1970; 245: 3917–27.
9.
DavidH.Hydrolysis by human α-amylase of p-nitrophenyloligosaccharides containing four to seven glucose units. Clin Chem1982; 28: 1485–9.
10.
TeshimaSHayashiYEmiSIshimaruK.Determination of α-amylase using a new blocked substrate (3-ketobutylidene β-2-chloro-4-nitrophenylmaltopentaoside). Clin Chim Acta1991; 199: 23–32.
11.
AbeANishimuraTNomaAHamanoK.Automated measurement of amylase isoenzymes by a kinetic assay with “blocked” β-2-chloro-4-nitrophenylmaltopentaoside as substrate and with wheat germ inhibitor. Clin Chem1991; 37: 1345–9.
12.
Winn-DeenESDavidHSiglerGChavezR.Development of a direct assay for α-amylase. Clin Chem1988; 34: 2005–8.
13.
SatomuraSSakataYOmichiKIkenakaT.α-Amylase assay with use of a benzyl derivative of p-nitrophenyl α-maltopentaoside, BG5P. Clin Chim Acta1988; 174: 314–24.
14.
KondoHShiraishiTNagataKTomitaK.An enzymatic method for the α-amylase assay which comprises a new procedure for eliminating glucose and maltose in biological fluids. Clin Chim Acta1988; 172: 131–9.
15.
BretaudiereJPRejRDrakePVassaultABaillyM.Suitability of control materials for determination of α-amylase activity. Clin Chem1981; 27: 806–15.