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PubMed1992

Further study of human salivary alpha-amylase polymorphism.

Genetic variants of salivary alpha-amylase were studied using isoelectric focusing in a pH gradient of 6-8 and silver staining methods. Five phenotypes which were tentatively named Amy1 N, Amy1 SN, Amy1 V1N, Amy1 V2SN and Amy1 V3N were detected. The phenotype frequencies in 371 unrelated Japanese were: Amy1 N = 94.33, Amy1 SN = 2.43, Amy1 V1N = 0.54, Amy1 V2SN = 0.27 and Amy1 V3N = 2.43%, respectively. Although variant bands of Amy1 V1N were detected by immunoblotting method using anti-human salivary amylase, those bands were not stained by starch-iodine method for the detection of amylase activity. This suggested that a mutation was occurred in the region of amylase molecule which showed the activity. Amy1 V2SN comprised the production of three Amy1 genes and indicated the duplication of Amy1 gene. The individuals showing Amy1 V3N phenotype accorded with those showing amylase variant by PAGE.

Electrophoresis, Polyacrylamide Gel↗
PubMed1976

[Mechanism of amylase action on glucoside starch bonds].

Functional groups of glucoamylase and alpha-amylase from Asp. awamori, alpha-amylase from Asp. oryzae and alpha- and beta-amylases from barley malt are identified. Kinetic curves of the activity dependency on pH, values of ionization heats and photooxidative inactivation draw to the conclusion that carboxyl-imidazole system enters into the active site of the enzymes. A hypothetic mechanism of hydrolysis of alpha-1,4-glucoside bond in starch molecule by alpha- and beta-amylases and of alpha-1,4- and alpha-1,6-glucoside bonds by glucoamylase is given. A theory of induced correspondence of enzyme and substrate satisfactorily explains the specificity of the enzyme action and the cause of complete starch convertion into glucose under glucoamylase action and of terminal starch hydrolysis by alpha- and beta-amylases.

Amylases↗
PubMed2004

[Concentration changes of amylase in vitreous humor of acute pancreatitis associated with different postmortem interval in rabbits].

OBJECTIVE: To investigate concentration changes of amylase in rabbits vitreous humor of acute pancreatitis associated with postmortem different interval. METHODS: To induce animal model of acute pancreatitis with sodium taurocholate, observed concentration changes of amylase after different postmortem interval, then compared with normal. RESULTS: The concentration of amylase in vitreous humor of rabbit 24h after death were related to postmortem interval significantly; The concluded formulae of the relationship between postmortem interval and amylase concentration is y=8.7420+0.7699x-0.0083x2 (R2=92.62792, F=14.89734, P=0.001). CONCLUSION: Concentration changes of amylase in vitreous humor of acute pancreatitis associated with postmortem interval may provide a new sensitive and objective method for the forensic early injury time estimation.

Amylases↗
PubMed2004

Extracellular amylase(s) production by fungi Botryodiplodia theobromae and Rhizopus oryzae grown on cassava starch residue.

The fungi Botryodiplodia theobromae and Rhizopus oryzae produce extracellular amylase when grown on a liquid medium containing 2% (WN) soluble starch or cassava starch residue(CSR) (as starch equivalent), a waste generated after extraction of starch from cassava, as the sole carbon source. Using CSR as the sole carbon source, the highest amylase activity of 3.25 and 3.8 units (mg, glucose released x ml(-1) x h(-1)) were obtained in shake flask cultures during the late stationary phase of growth of B. theobromae and R. oryzae, respectively. These values were slightly lower than the values obtained using soluble starch as the carbon source. Maximum enzyme synthesis in CSR incorporated medium occurred at the growth temperature of 30 degrees C and pH 6.0. Presence of inorganic NH4+ salts like ammonium acetate and ammonium nitrate in culture medium yielded more amylase than the other nitrogen sources. Amylase(s) production in the controlled environment of a Table-Top glass Jar Fermenter (2-L capacity) was 4.8 and 5.1 units for B. theobromae and R. oryzae, respectively using CSR as the carbon substrate. It is concluded that CSR, a cheap agricultural waste obtained after starch extraction from cassava could replace soluble starch as carbon substrate for commercial production of fungal amylase(s).

Amylases↗
PubMed2005

An ELISA method for the identification of salivary amylase.

An ELISA method for the detection of salivary amylase in dried stains using a monoclonal anti-human salivary amylase antibody was developed. Studies demonstrated the assay to be sensitive down to 0.0002 Sigma units and showed a linear response between absorbance and salivary amylase activity between 0.002 and 0.2 units. The assay showed no cross reactivity with either commercially purchased human pancreatic or bacterial amylase. Sample studies utilizing swabs from several human body fluids showed that 100% of all saliva containing swabs (sixteen of sixteen) and 13% of non-saliva human body fluid swabs (eight of sixty-three) showed a net absorbance with the method. Of these eight non-saliva swabs yielding a net absorbance, none exceeded a salivary amylase activity of 0.003 units. In contrast, only three of the sixteen saliva-containing swabs (swabs produced from saliva diluted 1:5, 1:6, and 1:10, respectively) showed an activity below 0.2 units. Of these swabs, the 1:100 dilution showed the lowest activity (0.048). This value is still more than ten times that of the non-saliva containing swab with the highest activity.

Amylases↗
PubMed2005

Hydrolytic activity of alpha-amylase in anaerobic digested sludge.

Hydrolysis is usually considered to be a rate-limiting step in anaerobic digestion. For improving anaerobic solid waste treatments, it is essential to elucidate the mechanism of hydrolysis. In this study, alpha-amylase, one of the hydrolytic enzymes, was investigated for the elucidation of more precise mechanism of hydrolysis. Alpha-amylase activity of solid starch-degrading bacteria (SDB) was estimated through batch experiments with several different substrates and with distinction between cell-bound and cell-free alpha-amylase. Monitoring of newly isolated strains of SDB was done by fluorescence in situ hybridization. Results indicated that cell-bound alpha-amylase is chiefly responsible for the hydrolysis in the digested sludge, providing very useful information that the contact between microbial cells and solids is significantly important. The activity of alpha-amylase of the digested sludge remained quite low when not required, but increased as they recognized appropriate substrates. Several-fold higher activity was obtained for starch or maltose as compared to glucose only.

Aeromonas↗
PubMed2005

A amylase activity of nymphal stages of sunn pest, Eurygaster integriceps Puton (Hemiptera: Scutelleridae).

Wheat production in Iran has changed substantially over the past one or two decades with development of higher-yielding cultivars and improved methods of planting. Sunn pest, Eurygaster integriceps (Heteroptera: Pentatomidae), is the most important cereal pest in Iran. Sunn pest like other insect pests of wheat lives on a polysaccharide-rich diet and depends to a large extent on effectiveness of their alpha-amylases for survival. alpha-amylase (1-4-alpha-D-glucan glucanohydrolase) hydrolyses starch, and related polysaccharides by randomly cleaving internal alpha-1,4-glucosidic linkages and has a major role in the utilization of polysaccharides. The recent increase in study of insect digestive enzymes seems to make sense in the realization that the gut is the major interface between the insect and its environment. Hence, an understanding of digestive enzyme function is essential when developing methods of insect control such as the use of enzyme inhibitor's and transgenic plants to control phytophagous insects. The aim of the current study is to identify and characterize alpha-amylase activity in order to gain a better understanding of its digestive physiology, which hopefully will lead to new strategies of the insect control. In order to analyze a-amylase activity adult and different nymphal stages were collected from wheat field from Karaj area and midgut complex from these individuals were dissected under a light microscope in ice-cold saline buffer (0.006M NaCl). After homogenization in buffer, homogenate was centrifuged at 15000 g for 20 min at 4 degrees C. The supernatant was pooled and stored at -20 degrees C for subsequent analysis. alpha-amylase activity was assayed by the dinitrosalicylic acid (DNS) procedure using soluble starch as substrate (starch 1%). Our result showed that enzyme activities in different nymphal stages (first, second, third, fourth and fifth stadium) were 0.19, 0.78, 1.21, 1.23, 1.25 units/mg protein, respectively.

Animals↗
PubMed2001

[The comparison of properties of alpha-amylase from the third and fourth stage of Anisakis simplex larvae].

alpha-Amylase is present in the third (L3) and in the fourth-stage (L4) of larvae from Anisakis simplex. The enzymes from both sources differ in some of their properties. alpha-Amylase from L3 showed a maximum at pH 7.8, enzyme from L4 stage at pH 6.5. The alpha-amylase from L3 was mainly lysosomal enzyme. The enzyme from L4 was located in the microsomal fraction. The L3 alpha-amylase showed the inhibition by EDTA and by -SH reagent iodoacetic acid. These agents did not change the activity of L4 enzyme. Both izoenzymes were unaffected by calcium and magnesium ions. Generally the alpha-amylase from L4 stage had higher activity (3.71 u/mg) than L3 one (2.29 u/mg).

Animals↗
PubMed1990

Amylase-producing plasmacytoma cell lines, AD3 and FR4, with der(14)t(8;14) and dic(8)t(1;8) established from ascites.

We established two human plasma cell lines, FR4 and AD3, from ascitic fluid in a patient with IgA k plasmacytoma (PC). Aberrant amylase production was found in this patient. Both AD3 and FR4 were free of Epstein-Barr virus, and both produced Ig A k in vitro. They produced amylase of the salivary type in vitro. This was confirmed by the demonstration of amylase mRNA comigrating with salivary gland mRNA. These cell lines commonly had unusual chromosomal abnormalities der(14)t(8;14) and dic(8)t(1;8). AD3 had additional chromosomal abnormalities compared with FR4. This suggests that AD3 is a subline of FR4. The oncogene c-myc is rearranged in most case of Burkitt's lymphoma with t(8;14). However, neither rearrangement nor amplification of the c-myc allele was detected in our PC lines. These lines expressed c-myc of 2.4 kb. There were no structural changes in the amylase genes of AD3 and FR4 detectable with Southern blotting analysis. As these lines were authentic PC lines, they would be useful for the future study of the relationship between the mechanism of oncogenesis and the rare tumor aberration, amylase production.

Aged↗
PubMed1990

[Ectopic production of amylase by a non-producing type of multiple myeloma].

The patient was a 64-year-old woman who was admitted to our hospital because of lumbago. A diagnosis of multiple myeloma (non-producing type) was made, based on (1) the presence of multiple osteolytic lesions, (2) hypercellular marrow with 64.2% plasmacytoid malignant cells, (3) no monoclonal gamma-globulin was detected in the serum and urine, and (4) abnormal monoclonal gamma-globulin was also not detected in the cytoplasm and membranes of these malignant cells. After several courses of chemotherapy, a pleural effusion infiltrated by myeloma cells developed and the patient's serum contained a markedly increased amylase activity of salivary-type. Amylase activity was also detected in vitro in the supernatant of cultured myeloma cells established from the patient's pleural effusion. The presence of alpha-amylase in the myeloma cells, which were derived from pleural effusion, was demonstrated immuno-histochemically. These observations indicates that amylase was ectopically produced by these myeloma cells. Interestingly, 14 out of 20 metaphases in the cells derived from pleural effusion showed translocation of 1p22 near the region of 1p21, where the amylase gene was assigned.

Amylases↗
PubMed1990

Relationships between pleural fluid pH, PCO2 to pleural fluid PO2, amylase, protein, glucose and white cells in tuberculous and malignant effusions.

The relationships between pleural fluid pH and PO2 to pleural fluid PO2, amylase, protein, glucose, white cell count were examined in 110 cases of tuberculous and 140 cases of malignant pleural effusions. Pleural fluid amylase concentrations of 200 or more units/ml indicated malignant effusions rather than tuberculous effusions with a specificity of 92.7 per cent and sensitivity of 27.1 per cent. There was evidence which suggested that the increasing pleural fluid amylase concentrations were due to the excessive leakage of serum amylase into the pleural cavity secondary to the break-down of capillaries by tuberculosis and malignancy as well as the production of amylase by tumor cells invading the pleura. The decreasing pleural fluid pH and increasing pleural fluid PCO2 had a significant linear relationship with decreasing fluid PO2, increasing pleural fluid protein and decreasing fluid glucose. These indicated a leakage of serum protein into the pleural cavity and the over-utilization of glucose relative to the transport defect of low pleural fluid glucose concentrations in the acidotic fluid of tuberculous and malignant effusions. No relationship between pleural fluid pH and PCO2 to pleural fluid and white cell count was found in the present study.

Adult↗
PubMed2006

[Cloning of the gene encoding a thermostable alpha-amylase from bacillus licheniformis CICIM B0204 and functional identification of its promoter].

Thermostable alpha-amylase, catalyzing the hydrolyzation of starch to dextrin, maltose and glucose at higher temperature, is one of the most industrial important enzymes. Several species of Bacillus have been found and genetic improved to produce the thermostable alpha-amylases. In present study, a gene, amyL, coding for a thermostable alpha-amylase with its flanking sequences was cloned from an industrial Bacillus licheniformis CICIM B0204 by using a combination of routine polymerase chain reactions (PCR) and inverse PCR with a pair of initial primers derived from the highly conserved region of bacterial alpha-amylase genes and the functional identifications of the cloned amyL and the activities of its promoter and signal peptide in Escherichia coli were investigated. The amyL was composed of 1539 bp with 180 bp at upstream for its promoter and 160 bp at downstream for its terminator. The deduced mature peptide of the a-amylase was composed of 512 amino acid residues and its signal peptide 29 amino acid residues at N-terminal. The nucleotide and deduced amino acid sequences of amyL were extremely similarity to those from Bacillus species with three amino acid residues difference (Arg163-->Leu, Ser339-->Gly, Ala349-->Ser) comparison to that from a laboratory strain B. licheniformis 584. Under the control of T7 promoter, the structural region of amyL was functionally expressed in Escherichia coli. Additionally, the structural region of the gene coding for a beta-mannosidase from B. licheniformis CICIM B2004 was inframely inserted into the downstream of the promoter and signal sequence of amyL and expressed in E. coli. The amyL promoter and signal sequence was functionally directed the expression and secretion of the beta-mannosidase in E. coli cells with the expression level of 295 U/mL.

Bacillus↗
PubMed1991

The value of pancreatic pseudocyst amylase concentration in the detection of pseudocyst communication with the pancreatic duct.

The aims of the study were to compare the results of endoscopic retrograde cholangiopancreatography (ERCP) and percutaneous cystopancreatography (PCP) in the detection of the communication between the pancreatic pseudocyst and the pancreatic duct, and to assess the reliability of the increased amylase concentration in the pseudocyst content as an indicator of the existence of communication between the pancreatic pseudocyst and the pancreatic duct system. Forty-three patients were included in the study. Pseudocystic fluid content was obtained by percutaneous aspiration. Twenty-four patients had pseudocyst amylase concentrations above 64 Wolgemuth units (WU), and 19 patients had less than 64 WU. The communication between pseudocyst and the pancreatic duct was determined in 22 patients by ERCP and in 13 patients by PCP, all in the group with increased pseudocyst amylase concentration. Due to high sensitivity and specificity of pseudocyst amylase concentration for the existence of pseudocyst communication with the pancreatic duct, we conclude that guided percutaneous aspiration of the pancreatic pseudocyst with the determination of amylase concentration in the fluid can replace ERCP as a method of choice for the detection of pseudocyst communication with the pancreatic duct.

Adult↗
PubMed1991

Automated measurement of amylase isoenzymes by a double kinetic assay with "blocked" beta-2-chloro-4-nitrophenyl maltopentaoside as substrate and with wheat germ inhibitor.

We evaluated the enzymic mechanism by which 3-keto butylidene-beta-2-chloro-4-nitrophenyl maltopentaoside (3KB-G5-CNP) serves as a substrate for serum pancreatic (p-) and salivary (s-) amylases. In aliquots of the reaction mixture, three kinds of beta-2-chloro-4-nitrophenyl oligosaccharides (glucose, maltoside, and maltotrioside) were separated from the substrate by high-performance liquid chromatography. Both isoenzymes behaved nearly identically and produced almost the same products. We automated a double kinetic procedure for determining total (t-) and p-amylase with use of a selective inhibitor from wheat germ in a single channel on the Hitachi 7050 analyzer. Within- and between-run CVs were, respectively, 0.5% and 1.7% for t-amylase (240 U/L), and 0.7% and 2.3% for p-amylase (230 U/L). The test results varied linearly with concentrations up to approximately 2000 U/L for t- and p-amylase activities. p/s ratios varied from 0.2 to 5.0. Results correlated well with those obtained by the monoclonal inhibition method (r = 0.992).

Amylases↗
PubMed1991

[Determination of fecal alpha-amylase activity in the diagnosis of chronic duodenitis].

Amylasorrhea has been detected in 92-97 percent of 190 patients suffering from chronic duodenitis, 40 of these children and 50 ones with concomitant imbalance of colonic microflora, during acutely or moderately manifest catarrhal and erosive mucosal abnormalities. This condition was somewhat more marked in the children and in the patients with colonic microflora imbalance, but less acute than in acute intestinal dysfunctions such as dysentery. A characteristic feature of duodenitis-associated amylasorrhea is the predominance of a thermolabile pancreatic fraction of amylase (a small-intestinal component of amylase); in cases with concomitant colonic microflora imbalance the share of thermostable intestinal fraction (amylase large-intestinal component) grows reaching its maximum in dysentery. In chronic duodenitis amylasorrhea is regularly detectable over the course of many years; whereas in dysentery it is more manifest though not lasting. Transient impaired membranous digestion involving a reduction of the intestinal surface to adsorb pancreatic amylase appears to be responsible for duodenitis associated amylase thin-intestinal component.

Adolescent↗
PubMed1991

Amylase-producing multiple myeloma.

We managed a case of amylase-producing multiple myeloma with extensive extramedullary spread. We reviewed five cases of amylase-producing multiple myeloma, including this case. This type of multiple myeloma has shown unique clinicopathologic features. (1) A distinct elevation of the serum amylase activity was demonstrated in all five patients. The amylase isozyme was of the S type without exception. (2) Extensive extramedullary spread with extramedullary tumors and/or myelomatous pleural effusions or ascites was seen in all five patients during the course of illness. (3) In three of four cases in which it was mentioned, extensive destruction of multiple bones was demonstrated roentgenographically. (4) In four patients, excepting one with a solitary bone lesion, the survival from the initial therapy was shorter than 1 year. (5) Myeloma cell lines were established in three cases. A common feature of these three cell lines was a translocation of chromosome 1, which supplied the amylase gene. This finding may be pathogenetically related to this entity.

Aged↗
PubMed1991

Non-parallel secretion of pancreatic amylase and trypsinogen following hepatectomy in rats.

To explore the changes in exocrine pancreatic function in the stages of active regeneration and recovery after hepatectomy, we measured the caerulein-stimulated amylase and trypsinogen output in anesthetized rats 4 days and 8 days after about 70% hepatectomy. Both 4 days and 8 days after hepatectomy, the amylase output was significantly greater than in the control groups. On the other hand, 4 days after hepatectomy, the trypsinogen output was almost the same as in the control groups, and 8 days after hepatectomy, it was significantly lower than in the control groups. Thus, the secretion of amylase and trypsinogen 8 days after hepatectomy was not parallel. The amylase content of the pancreas was significantly larger after hepatectomy than in the control groups, but the trypsinogen content was significantly smaller. These results indicate a non-parallel secretion of pancreatic digestive enzymes, as well as differences in the functions of the acinar cells after partial hepatectomy, and the important role of amylase in glucose metabolism after hepatectomy.

Amylases↗
PubMed1991

[Effect of antibodies on the catalytic properties of bacillary alpha-amylase].

The interaction between bacillar alpha-amylase and polyclonal antibodies was studied. It was found that the dependence of the enzyme activity on antibody concentration is biphasic, being increased at low concentrations of the antibodies with a further decline down to complete inhibition at their high concentrations. Starch hydrolysis by amylase-antibody complexes was characterized by the growth of the formation glucose and triglycoside. These results are consistent with theoretical calculations of the antigenic determinant localization relative to components of the enzyme active center. Starch hydrolysis by amylase complexes with immobilized antibodies was also studied. A method of amylase detection with the help of the given system was developed. It was demonstrated that reactions between amylase-hormone (estradiol, testosterone) conjugates and hormone-specific antibodies also change the levels of the amylolytic activity.

Antibodies↗