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α-AMYLASE Assay Kit
The α-Amylase Test Kit is intended for the quantitative determination of α-amylase activity. Cat.No: OttoBC125
Product Description
The a‑amylases (1,4‑a‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycol‑ gen by cleaving 1,4‑a‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of a‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ‑specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube. Because of the sparsity of specific clinical symptoms of pancreatic diseases, aamylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyper‑ amylasemia does not, however, only occur with acute pancreatitis or in the inflam‑ matory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreasspecific enzyme ‑ lipase or pancreatic‑a‑amylase‑ also be determined. Numerous methods have been described for the determination of a‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑ catalyzed subsequent reactions. The kinetic method described here is based on the cleavage of 2‑chloro‑4‑nitrophenyl‑aDmaltotrioside (CNP‑G3) by a‑amylase.
Contents
Colorimetric test with 2‑chloro‑4‑nitrophenyl‑a‑D‑maltotriose (CNP‑G3) as direct substrate. Colour is released directly as a result of a cleavage at the aglycone:
CNP ‑ G3→ CNP + G3
The increase of absorption of chloro‑nitrophenol is directly proportional to the a‑ amylase concentration. The hydrolysis pattern in the formulation of the reagent show about less than 10 % CNP‑G2 and less than 1% CNP‑G4 as by products.
Referanslar
1. Bertholf RL, Winn‑Deen ES, Bruns DE. Amylase in urine as measured by a single ‑step chromolytic method. Clin Chem 1988; 34: 754‑7
2. Fenton J, Foery R, Piatt L, Geschwindt K. A new chromogenic amylase method compared with two established methods. Clin Chem 1982; 28: 704‑ 6.
3. Glick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470‑474
4. Greiling H, Gressner AM ed. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3. Auflage. Stuttgart/New York: Schattauer Verlag, 1995. 5. Keller H ed. Klinisch‑ chemische Labordiagnostik für die Praxis, 2. Auflage. Stuttgart/New York: Georg Thieme Verlag, 1991 ;354‑361.
6. Lorentz K. Approved Recommendation on IFCC Methods for the Measurement of Catalytic Concentration of Enzymes. Part 9. IFCC‑Method for a‑Amylase (1,4‑a‑D‑Gluca 4‑Glucano‑ Hydrolase, EC 3.2.1.1.). Clin Chem Lab Med 1998;38:195‑203
7. Rauscher E et al. Fresenius Z Analyt Chem 1986; 324:304.
8. Salt WB II, Schenker S. Amylase‑its clinical significance: a review of the literature [Review]. Medicine 1976; 55:269‑281 .
9. Steinberg WM, Goldstein SS, Davies ND et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985; 102:576 ‑ 580.
10. Tietz NW ed.: Clinical Guide to Laboratory Tests. 3. Auflage. Philadelphia, PA: W B Saunders Company; 1995:46‑51 Tietz NW, Huang WY, Rauh DF et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32:301‑307
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