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PubMed1997

[Investigation of alpha-amylase denatured by urea and guanidine hydrochloride. I. Studies on denaturation mechanism and renaturation efficiency by high-performance hydrophobic interaction chromatography].

The varieties of alpha-amylase denatured with 8.0 mol/L urea and 7.0 mol/L guanidine hydrochloride (GuHCl) solutions and their refolded intermediates were separated and renatured through high performance hydrophobic interaction chromatography (HPHIC). With investigating and comparing the numbers of the refolded intermediates and the bioactivity recovery of renaturation by means of HPHIC, it was found that these are quite different. The results can be attributed to the different denaturation mechanism of alpha-amylase with the two denaturing agents. The numbers of the refolded intermediates of urea-unfolded alpha-amylase were found to be more than that denatured by GuHCl, because GuHCl may make the changes in the surface of alpha-amylase molecules, by contrast, urea may do the changes not only in the surface of the protein, but also in the hydrophobic packet interior of the molecules. The HPHIC packings with weak hydrophobicity was found to have good separation efficiency and to have almost continuous and many peaks denoting these intermediates, while that with strong hydrophobicity was found to have higher bioactivity recovery. The numbers of the intermediates of urea-unfolded alpha-amylase were much more than that of bovine pancreatic trypsin inhibitor (BPTI) separated by Weissman et al. The effect of temperature on the separations and the renaturations were investigated too. The result showed that the higher the column temperature, the more the refolded intermediates of unfolded alpha-amylase separated and the lower bioactivity recovery were obtained from HPHIC.

Animals↗
PubMed2005

Biochemical analysis of serum pancreatic amylase and lipase enzymes in patients with type 1 and type 2 diabetes mellitus.

OBJECTIVE: To examine the pancreatic exocrine insufficiency in patient with diabetes mellitus by estimating serum pancreatic amylase and lipase enzymes in healthy subjects and in type 1 and type 2 diabetic patients. METHODS: The study was conducted on 20 normal healthy volunteers and 39 diabetic patients referred to Al-Isra Medical Laboratory, Amman, Jordan during the period from April - November 2003 after recording their age and gender. The age of onset of diabetes and the type of treatment were determined and the patients were categorized into type 1 and type 2 diabetics. Blood samples were collected and analyzed for fasting blood sugar (FBS), glycosylated hemoglobin (HbA1C), serum insulin, and serum pancreatic amylase and lipase enzymes. All biochemical tests were carried out in the medical laboratories of Islamic Hospital, Amman, Jordan. All estimates were presented as means +/- SD, and statistical treatment of data were performed using student t-test. RESULTS: The FBS and HbA1C estimates were consistently higher in type 1 and type 2 diabetic patients, while no significant changes were observed in the estimates of serum insulin between the normal and diabetic patients. The reduction in serum pancreatic amylase was recorded in both types of diabetes, which amounted to 71% for type 1 diabetics and 49% for type 2 diabetics. On the other hand, reduction in serum lipase was only detected in type 1 diabetics amounting to 31%. Correlation of the reduction in serum amylase and lipase levels with the duration of disease revealed a remarkable decrease in both enzymes in patients with long-standing disease (76% and 39%) in type 1 diabetic patients. Whereas, patients with very low serum insulin estimates the reduction in serum amylase was 77% while serum lipase level was reduced by 42%. Similarly, the reduction in serum amylase in type 2 diabetes was higher in patients with longer duration of illness (59%) and in patients with low serum insulin value (79%), while reduction in serum lipase was only detected in patients with very low serum insulin (34%). No differences in all measured parameters between males and females were recorded in type 1 and type 2 diabetics. CONCLUSION: Although most of diabetic research has been focused on dyslipidemia as a major risk factor for cardiac, cerebral and renal complications, the present study clearly illustrates an impairment of pancreatic exocrine function in type 1 and type 2 diabetes. We suggest that analysis of serum pancreatic enzymes could be an additional informative parameter for the assessment of chronicity and progress of the illness as well as the response to therapy.

Adult↗
PubMed2004

Polymorphism of the serum alpha-amylase in the population of the South Central and South Eastern regions of Bulgaria and its relationship with the erythrocyte blood group systems ABO and MNSs.

INTRODUCTION: The goal of the study was to investigate the relationship between the polymorphism of alpha-amylase and the erythrocyte systems--ABO, MNSs, and determine their population distribution and individual phenotype and gene incidence. MATERIAL AND METHODS: Parallel examinations of identical blood samples were carried out to determine the phenotypes of alpha-amylase and ABO and MNSs blood group systems. Blood was obtained by venipuncture in the Serological Laboratory of the Department of Forensic Medicine at the Medical University of Plovdiv. Amylase phenotypes were determined by the authors' own modification of Kompf's method using continuous horizontal electrophoresis of blood serum on agarose gel. Only the classical phenotypes of the examined blood group systems--alpha-amylase, ABO and MNSs were determined in the study. RESULTS. The analysis of the data by chi-square analysis using Pearson criterion found no relationship between the polymorphism of the serum alpha-amylase and ABO and MNSs erythrocyte systems. The allele frequencies determined were 1(a) = 0.9595, 1(b) = 0.0388, 1(o) = 0.0017 for Amyl and 2(a) = 0.9579 and 2(b) = 0.0421 for Amy2. CONCLUSION: The difference between the observed and expected phenotypes of the examined blood group systems alpha-amylase, ABO, MNSs is short of statistical significance. This indicates genetic stability of the examined blood group systems in the studied population.

ABO Blood-Group System↗
PubMed2005

[Expression of acidophilic alpha-amylase from Alicyclobacillus acidocaldarius].

The alpha-amylase (EC 3.2.1.1) from the Gram-positive Alicyclobacillus acidocaldarius was one kind of thermoacidophilic enzyme, with optimal temperature and pH of 75 degrees C and 3, respectively. The nucleotide sequence of the gene amy was cloned by PCR. The gene amy was 3901bp long, comprising one open reading frame encoding a polypeptide of 1301 amino acids. The calculated molecular weight of the alpha-amylase AMY was about 140kD. The gene amy was expressed in E. coli BL21 (DE3) and Pichia pastoris respectively, and both of the cloned proteins had bioactivity. The activity of amylase expressed in P. pastoris was further testified by amylase activity staining. The alpha-amylase expressed in P. pastoris had been purified and characterized. The apparent molecular weight of that was about 160kD according to SDS-PAGE. The optimum of pH for the enzyme was pH 3.2 as the native enzyme was; but the optimum of temperature was 65 degrees C and a little lower than that of the native enzyme. Above 50% of relative activity remained after incubation for 30 minutes in 70 degrees C. So the enzyme expressed by P. pastoris was also thermoacidophilic. Moreover some sequence was cloned by PCR, which ranged from + 1174 bp to + 3288 bp in the gene amy, encoding 705 amino acids with the calculated molecular weight of 79kD. The truncated gene amy' was expressed in E. coli BL21 (DE3) induced by 1 mmol/L IPTG, and the expressed enzyme also retained alpha-amylase activity.

Bacillus↗
PubMed2006

[Expression of the gene coding for a thermostable alpha-amylase from Pyrococcus furious in Chiamydomonas reinhardtii chloroplast ].

Thermostable alpha-amylase from Pyrococcus furious is an important industrial enzyme in brewing and alcohol production. Eexpression of the thermostable a-amylase in plants can reduce greatly costs in the production of alcohol using crop plants. A chloroplast expression vector, p64A, containing the thermostable alpha-amylase gene from Pyrococcus furious, was constructed with clpP-trnL-petB-chlL-rp123-rpl2 as Chlamydomonas reinhardtii plastid homologous recombinant fragments and spetinomycin-resistant aadA gene as select marker. The plasmid p64A was transferred into the chloroplast genome of C. reinhardtii by the biolistic method. Nine independently transformed lines were obtained by 100 mg/L spectinomycin selection. PCR amplification, Southern blot analysis of the transgene and cultivation in the dark all showed that the a-amylase gene had been integrated into chloroplast genome of C. reinhardtii. The activity of amylase expressed in the chloroplast of C. reinhardtii was detected by amylase activity assay and found to be as high as 77.5 u/g fresh weight of cells. These experimental results demonstrated the possibility of using transgenic chloroplasts of plant as bioreactors for production of industrial enzymes.

Chlamydomonas reinhardtii↗
PubMed1990

[Amylase-producing extramedullary plasmacytoma with multiple cutaneous metastasis following a solitary plasmacytoma of bone].

A 65-year-old woman was admitted because of multiple cutaneous tumors in the left lumbar area in March 1983. In 1979, she had been diagnosed as solitary plasmacytoma (IgG, kappa) of the left femur and amputation of the left leg had been performed. In 1981, the tumor relapsed in the left ilium in association with an increased level of serum IgG with M-component and normal activity of serum amylase. The serum M-protein had been disappeared after resection of the tumor. On admission laboratory examinations showed a slightly high level of serum IgG and elevated activities of serum and urine amylase. Amylase isoenzyme analysis revealed a predominance of the S-isozyme. Bone marrow aspiration revealed no atypical plasma cells. The supernate of cultured plasma cells obtained from the cutaneous tumor contained high amylase activity consisting exclusively of S-type. Thereafter serum amylase activities changed approximately in parallel with serum M-protein levels and total tumor volumes after chemotherapy or radiotherapy. At the terminal phase in 1986, however, serum amylase activities became extraordinarily high compared with serum M-protein levels, suggesting a clonal change of the plasmacytoma cells.

Aged↗
PubMed1991

Diagnostic and prognostic utility of phospholipase A activity in patients with acute pancreatitis: comparison with amylase and lipase.

We compared the diagnostic and prognostic utility of phospholipase A (PLA; EC 3.1.1.4) for acute pancreatitis with that of amylase and lipase by analysis of sera from 151 consecutive patients presenting with abdominal pain in whom assays of serum amylase and (or) lipase had been ordered. We determined the diagnostic accuracy for both the initial and the peak enzyme activities. Maximal diagnostic accuracy obtained for the initial activities of amylase, lipase, and PLA was 0.83, 0.83, and 0.76 at cutoff values of 650, 650, and 41 U/L, respectively. Use of peak enzyme activities showed maximal diagnostic accuracy of 0.85, 0.86, and 0.73 at cutoff values of 650, 1050, and 42 U/L, respectively. Receiver-operator characteristic curve analysis revealed the diagnostic performance of amylase and lipase to be similar, whereas that of PLA was almost random and not incremental. As with amylase and lipase, PLA activities in sera showed no relation to patients' survival; three patients who died after an attack of acute pancreatitis failed to demonstrate the dramatic increases in PLA activity previously described. We conclude that assessing the severity of acute pancreatitis by using enzyme activities still remains problematical. Measurements of amylase or lipase activities provide similar diagnostic discrimination when appropriate cutoff values are used and remain the methods of choice for diagnosis of acute pancreatitis.

Acute Disease↗
PubMed1991

Lipase isoforms and amylase isoenzymes: assays and application in the diagnosis of acute pancreatitis.

Pancreatic juice and serum from patients with acute pancreatitis contain three enzymes that have lipolytic activity: L1 and L2, which are pancreatic isoenzymes or isoforms of lipase (EC 3.1.1.3), and L3, which is probably pancreatic carboxyl ester lipase, also known as cholesterol esterase (EC 3.1.1.13). These enzymes are readily separated electrophoretically on agarose and can be developed with an overlay of Kodak Ektachem lipase slide material. The latter acts as a dry-reagent developing substrate, with the enzymes producing blue bands in the slide material. We found L1 in about one-half of normal persons, L2 in none, and L3 in all. We assayed for amylase (EC 3.2.1.1), amylase isoenzymes, lipase, and lipase isoforms in the sera of 100 patients with suspected acute pancreatitis. L2 lipase has the greatest diagnostic efficiency for the diagnosis of pancreatitis, compared with total amylase, P3 amylase, and total lipase. Lipase and L2 could replace amylase, an inefficient test, for the diagnosis of patients with suspected acute pancreatitis. In patients receiving organ transplants, a serum amylase value of greater than 300 U/L or a lipase of greater than 1000 U/L discriminated well between patients with and without complications and (or) acute rejection.

Acute Disease↗
PubMed1990

[Baking ingredients, especially alpha-amylase, as occupational inhalation allergens in the baking industry].

Baker's asthma is the most frequent occupational lung disease in Switzerland and West Germany. Cereal flours, and more rarely flour parasites, are implicated as the responsible allergens. Based on an observation of a case of baker's asthma due to monovalent sensitization to alpha-amylase used as additive to flour, 31 bakers with occupational asthma and/or rhinitis were routinely tested by skin tests and serological RAST examinations for allergic sensitivity to flour, alpha-amylase and other bakery additives. 17/31 subjects (55%) reacted positively in scratch tests to a commercial powdered alpha-amylase and 13/20 (65%) to a lecithin preparation. 23/31 (74%) and 19/31 (61%) were RAST positive to wheat and to rye flour respectively. 32% had RAST specific IgE to alpha-amylase (from Aspergillus oryzae), 19.3% to soya bean flour and 16% to malt. 7/12 and 5/12 respectively reacted to trypsin inhibitor and lipoxidase, the main allergens in soya bean. In two patients monosensitization to alpha-amylase was present. In accordance with other reports we recommend that baking additives, especially alpha-amylase, should be tested in allergological diagnosis of occupational diseases in flour processing workers. Full declaration of all additives used in the bakery industry is needed.

Adolescent↗
PubMed1985

Role of free cytosolic calcium in secretagogue-stimulated amylase release from dispersed acini from guinea pig pancreas.

To determine the role of free cytosolic calcium ([Ca+2]i) in stimulated enzyme secretion from exocrine pancreas, we determined the effects of various pancreatic secretagogues on [Ca+2]i and amylase release in dispersed acini from the guinea pig pancreas. Cholecystokinin-octapeptide (CCK-OP), carbachol, and bombesin, but not vasoactive intestinal peptide, stimulated rapid increases in [Ca+2]i from 100 to 600-800 nM that were independent of extracellular calcium. The increases in [Ca+2]i were transient (lasting less than 5 min) and correlated with an initial rapid phase of amylase release. After 5 min, secretagogue-stimulated amylase release occurred at basal [Ca+2]i. Carbachol pretreatment of the acini abolished the effects of CCK-OP and bombesin on [Ca+2]i and the initial rapid phase of amylase release. 4 beta-phorbol 12-myristate 13-acetate (PMA) had no effect on [Ca+2]i but stimulated an increase in amylase release. The addition of CCK-OP or A23187 to PMA-stimulated acini caused an increase in [Ca+2]i and PMA-stimulated amylase release only during the first 5 min after addition of these agents. These results indicate that CCK-OP, carbachol, and bombesin release calcium from an intracellular pool, resulting in a transient increase in [Ca+2]i and that this increase in [Ca+2]i mediates enzyme secretion during the first few minutes of incubation. The results with PMA suggest that secretagogue-stimulated secretion not mediated by increased [Ca+2]i (sustained secretion) is mediated by 1,2-diacylglycerol.

Amylases↗
PubMed1986

Salivary amylase and pancreatic enzymes in serum after total body irradiation.

Amylase increases in serum after total body irradiation (TBI). To investigate whether this increase is ascribable to pancreatic or salivary amylase, or both, we measured the post-irradiation activity concentration of the three major pancreatic enzymes (trypsin, amylase, and lipase) and of salivary-type amylase in serum from six leukemic patients given TBI before bone-marrow transplantation. Salivary amylase increased by as much as 50-fold after TBI, peaking on the first day after the irradiation. The increase was associated with the development of clinical parotitis. Pancreatic trypsin, total amylase, and lipase increased inconsistently and to a much smaller degree. There were no associated clinical features of pancreatitis. Our data show that, at the dose of radiation given to our patients, there is no danger of pancreatitis as a complication, but parotitis is a consistent development after TBI.

Amylases↗
PubMed1986

Amylase.

The laboratory determination of serum and urine amylase activity is commonly requested by the Emergency physician. While depressed levels are occasionally seen, they are almost always secondary to chronic pancreatitis and pancreatic destruction. The typical abnormality is an elevation that may represent a normal physiologic process, a benign inflammation, the concomitance of ongoing disease, or an emergent problem. The differential diagnosis of hyperamylasemia is difficult, but most high levels are caused by pancreatitis and biliary tract disease. Serial determinations of amylase levels, as well as simultaneous assessments of urine and serum amylase, may be useful in determining the source of the problem. The laboratory methods for measurement are many and varied, reflecting the lack of a perfect test. Because of the different procedures, confusion has ensued over the units of description and the normal or reference ranges. Any standard equipped medical laboratory should be able to determine amylase activity in both serum and urine in a timely fashion. The average cost per amylase determination is $17.75. The actual time to perform the test in the laboratory is approximately 7.5 minutes, though turnaround times usually exceed 1 hour. The fractionation of amylase into isoenzymes is a sophisticated procedure requiring equipment not routinely found in a typical hospital laboratory.

Amylases↗
PubMed1987

CR-1409: a potent inhibitor of cholecystokinin-stimulated amylase release and cholecystokinin binding in rat pancreatic acini.

The effects of a new glutaramic acid derivative, 3,4-dichloro-benzamido-N, N-dipentyl-glutaramic acid (CR-1409), on cholecystokinin-stimulated amylase release and 125I-cholecystokinin octapeptide binding were studied in isolated rat pancreatic acini. CR-1409 at concentrations between 0.3 and 30 microM inhibited cholecystokinin-stimulated amylase release in a dose-dependent manner without appreciable effect on the basal amylase secretion. Biphasic dose-response curves to cholecystokinin for amylase release shifted to the right with an increase in the concentration of the drug. IC50 (half-maximal inhibitory concentration) of CR-1409 for cholecystokinin-stimulated amylase release was 0.64 microM, and the potency of this drug on the inhibition of amylase release was 3400 times greater than that of proglumide. The effect of CR-1409 was rapid, reversible, and selective for cholecystokinin. In addition, CR-1409 at concentrations between 0.1 and 30 microM inhibited 125I-cholecystokinin octapeptide binding to rat pancreatic acini. IC50 of CR-1409 for 125I-cholecystokinin octapeptide binding was 0.22 microM, and the potency of this drug on the effect was 5900 times greater than that of proglumide.

Amylases↗
PubMed1988

Assay of pancreatic amylase with use of monoclonal antibodies evaluated.

To evaluate a new method for measuring pancreatic amylase in serum, in which the salivary isoenzyme is inhibited with a specific monoclonal antibody, we determined the activity of pancreatic and salivary amylase in sera from 103 healthy subjects and from 114 hospitalized patients having a wide range of total amylase activities. CVs for the proposed method ranged from 0.8% to 5.1% (within day) and from 2.3% to 6.6% (day to day). Results correlated well with those obtained by the wheat-germ inhibition method (r = 0.998) and by electrophoresis on cellulose acetate. Analytical-recovery studies confirmed the good specificity of the monoclonal antibody for salivary amylase (97%) and its low cross-reactivity (0.6%) toward pancreatic amylase. The assay procedure presents a wide range of linearity (141-1817 U/L) and can easily be adapted to an automated kinetic system. We found the proposed method suitable for routine determinations of pancreatic amylase.

Adult↗
PubMed1989

Age and sex-dependent changes in serum amylase in an apparently healthy population.

In order to determine whether changes in serum amylase are age- or sex-dependent, we evaluated age- and sex-stratified serum amylase values in subjects who were proven to be healthy by a precise preventive health examination. Results showed that serum amylase increased as age progressed, except in the 0- to 29-yr-old female group. Mean serum amylase was higher in females than in males. A previous study indicated that the etiology of the increase in amylase in elderly persons is due to a progressive decline in renal function with aging. The etiology of the sex difference, especially in the younger generation, requires further investigation. We should pay attention to the factor of age when we evaluate serum amylase.

Adolescent↗
PubMed1989

Circulating concentrations of trypsin-like immunoreactivity and activities of lipase and amylase after pancreatic duct ligation in dogs.

The possibility that assay of circulating trypsin-like immunoreactivity (TLI) could assist in the diagnosis of acute pancreatitis in dogs has been examined by assaying plasma TLI concentrations after pancreatic duct ligation and comparing the results with plasma activities of lipase and amylase. Venous blood samples were obtained from 8 dogs before surgery, then daily for 5 days and at 14 days after ligation of pancreatic ducts. Plasma concentrations of TLI increased within 24 hours and tended to peak before and to decrease more rapidly than activities of lipase and amylase, remaining greater than the control range for 5 days in all but 2 dogs. Plasma lipase and amylase activities increased together and remained greater than the control range in all dogs for 5 days after surgery. Regression analysis of all postoperative data indicated significant correlations between concentration of TLI and lipase activity (r = 0.67, P less than 0.001), concentration of TLI and amylase activity (r = 0.53, P less than 0.001), and between lipase and amylase activities (r = 0.74, P less than 0.001). These findings suggested that assay of TLI may provide an early indication of acute pancreatitis in dogs. Because TLI is specifically pancreatic in origin, high plasma TLI concentration may prove a more reliable indicator of clinical pancreatitis than high activities of amylase or lipase, which may be derived from extrapancreatic tissues.

Amylases↗
PubMed1985

Macroamylase immunoglobulins show high affinity for animal and human amylases.

We have examined the affinity shown by the immunoglobulin fraction from each of five sera containing macroamylase for amylases from different sources: human saliva or human, porcine, or ovine pancreas. High affinity constants, 0.4 X 10(10) to 7.2 X 10(10) L/mol, were found in competitive binding experiments with human or porcine pancreatic amylase. All but one serum yielded linear Scatchard plots, indicating that in most sera the amylase-binding immunoglobulins are homogeneous, possibly monoclonal. The immunoglobulin fractions from different sera differed in their specificity: two of them bound all four types of amylases, whereas two bound only one type. Three of the five immunoglobulin fractions showed considerably higher affinity towards one or both of the animal amylases than towards the human ones, and may be primarily directed against some animal amylase.

Amylases↗
PubMed1985

[Simultaneous production of amylase and adrenocorticotropin by lung cancer--with special reference to electron microscopic and immunohistochemical studies].

The tumor tissue from a lung cancer patient who showed elevated serum amylase and adrenocorticotropin was investigated ultrastructurally and immunohistochemically. On microscopic examination, the tumor was diagnosed as small-cell carcinoma. Electron microscopy revealed that some of the tumor cells possessed small endocrine-like dense cored granules. The tumor cells also contained large zymogen-like granules within the cytoplasm, which possessed microvilli and formed the lumen, indicating their adenocarcinomatous differentiation. An electrophoretic analysis of the serum amylase showed that the major amylase elevated was of the salivary type. Immunohistochemical staining by the antihuman salivary amylase antibody disclosed that various portions of the tumor actually contained the salivary amylase. The evidence suggests that the small-cell carcinoma cells showed "confused differentiation", thereby expressing amylase and ACTH simultaneously.

Adrenocorticotropic Hormone↗