Serum succinyltrialanine p-nitroanilide hydrolysing activity was elevated in patients with hepatobiliary diseases. The highest activities were seen in acute cholangitis and intrahepatic cholestasis. The change in succinyltrialanine p-nitroanilide hydrolysing activity was closely associated with those in γ-glutamyltranspeptidase and alkaline phosphatase activities. In some cases, however, the former was more sensitive than the latter.
References
1.
BarrettA. J.StrakeyP. M. (1973). The interaction of α2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. Biochemical Journal, 133, 709–724.
2.
BiethJ.SpiessB.WermuthC. G. (1974). The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biomedical Medicine, 11, 350–357.
3.
BrattonA. C.MarshallE. K.Jr. (1939). A new coupling component for sulfanilamide determination. Journal of Biological Chemistry, 128, 537–550.
4.
CoulombeJ. J.FavreauL. (1963). A new simple semimicro method for colorimetric determination of urea. Clinical Chemistry, 9, 102–108.
5.
The Enzyme Commission of the German Society for Clinical Chemistry. (1970). Recommendations of the German Society for Clinical Chemistry. Standardisation of methods for the estimation of enzyme activity in biological fluids. Zeitschrift für klinische Chemie und klinische Biochemie, 8, 659–660.
6.
FolinO.WuH. (1919). A system of blood analysis. Journal of Biological Chemistry, 38, 81–110.
7.
KatagiriK.ItoK.TeraoN.MiyajiM.ItoM.TakeuchiT.SasakiM. (1979). Significance of serum proteinases (trypsin-like and elastase-like enzymes) in hepatic and pancreatic diseases. (Abstract). Japanese Journal of Gastroenterology, 76, 1381.
8.
KindP. R. N.KingE. J. (1954). Estimation of plasma phosphatase by determination of hydrolysed phenol with amino-antipyrine. Journal of Clinical Pathology, 7, 322–326.
9.
MehlJ. W.O'ConnellW.DeGrootJ. (1964). Macroglobulin from human plasma which forms an enzymatically active compound with trypsin. Science, 145, 821–822.
10.
OgawaM.KosakiG.TanakaS.IwakiK.NomotoM. (1979). An activity of hydrolyzing elastase substrate succinyltrialanine p-nitroanilide in human bile. Clinica chimica acta, 93, 235–238.
11.
SaklatvalaJ. (1977). Hydrolysis of the elastase substrate succinyltrialanine nitroanilide by a metal-dependent enzyme in rheumatoid synovial fluid. Journal of Clinical Investigation, 59, 794–801.
