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At least 163 records · Page 9Linked to original sources
PubMed1988

Enzymatic synthesis of p-nitrophenyl alpha-maltopentaoside in an aqueous-methanol solvent system by maltotetraose-forming amylase: a substrate for human amylase in serum.

Transglycosylation from maltopentaose to the 4-position of p-nitrophenyl alpha-glucoside was efficiently induced through the use of maltotetraose-forming amylase from Pseudomonas stutzeri in an aqueous solution containing methanol at a high concentration. The enzyme specifically formed p-nitrophenyl alpha-maltopentaoside (12% of the enzyme-catalyzed net decrease of maltopentaose) from maltopentaose as a donor and p-nitrophenyl alpha-glucoside as an acceptor. The rate of the transglycosylation depended on the concentration of methanol solvent, the pH and the temperature. Use of the aqueous methanol system in this reaction not only ensured a sufficient solubility of p-nitrophenyl alpha-glucoside but also resulted in a remarkable increase in the formation of p-nitrophenyl alpha-maltopentaoside, which is a useful substrate for assay of human amylase in serum and urine.

Amylases↗
PubMed1980

Elevated amylase creatinine clearance ratio and normal serum amylase levels in chronic relapsing pancreatitis after partial pancreatectomy.

A 29-year-old woman admitted for alcohol detoxification five years after a 90% distal pancreatectomy for chronic pancreatitis had abdominal pain similar to that associated with preoperative pancreatitis. Although her clinical course was consistent with recurrent pancreatitis, the serum amylase level remained normal, but the amylase creatinine clearance ratio became elevated and then returned to normal, paralleling her clinical course. The ACCR may be a useful laboratory method in diagnosing chronic recurrent pancreatitis in patients with decreased functional pancreatic tissue.

Adult↗
PubMed1989

Two human myeloma cell lines, amylase-producing KMS-12-PE and amylase-non-producing KMS-12-BM, were established from a patient, having the same chromosome marker, t(11;14)(q13;q32).

Two human myeloma cell lines, KMS-12-PE and KMS-12-BM, were established from a 64-year-old woman with a non-producing type of multiple myeloma. The KMS-12-PE line originated from the pleural effusion and the KMS-12-BM from the bone marrow. These two lines showed the same chromosome marker, t(11:14)(q13:q32). However, their phenotypes of surface markers differed from each other. KMS-12-BM cells were positive to CD20, CD38 and PCA-1. showing the plasmacytoid (immature plasma cell) stage of B-cell differentiation, while KMS-12-PE cells were positive to CD38 and PCA-1, but not to CD20, indicating the terminal differentiated stage of B-cells. As seen in the pleural effusion of the patient. KMS-12-PE cells ectopically produced a salivary type of amylase, but KMS-12-BM cells did not. Interestingly, the chromosome abnormality of del(1)(p22----pter) near the region of 1p21, where the amylase gene was assigned, was noticed in as many as 76% of KMS-12-PE cells.

Amylases↗
PubMed2005

AmyA, an alpha-amylase with beta-cyclodextrin-forming activity, and AmyB from the thermoalkaliphilic organism Anaerobranca gottschalkii: two alpha-amylases adapted to their different cellular localizations.

Two alpha-amylase genes from the thermophilic alkaliphile Anaerobranca gottschalkii were cloned, and the corresponding enzymes, AmyA and AmyB, were investigated after purification of the recombinant proteins. Based on their amino acid sequences, AmyA is proposed to be a lipoprotein with extracellular localization and thus is exposed to the alkaline milieu, while AmyB apparently represents a cytoplasmic enzyme. The amino acid sequences of both enzymes bear high similarity to those of GHF13 proteins. The different cellular localizations of AmyA and AmyB are reflected in their physicochemical properties. The alkaline pH optimum (pH 8), as well as the broad pH range, of AmyA activity (more than 50% activity between pH 6 and pH 9.5) mirrors the conditions that are encountered by an extracellular enzyme exposed to the medium of A. gottschalkii, which grows between pH 6 and pH 10.5. AmyB, on the other hand, has a narrow pH range with a slightly acidic pH optimum at 6 to 6.5, which is presumably close to the pH in the cytoplasm. Also, the intracellular AmyB is less tolerant of high temperatures than the extracellular AmyA. While AmyA has a half-life of 48 h at 70 degrees C, AmyB has a half-life of only about 10 min at that temperature, perhaps due to the lack of stabilizing constituents of the cytoplasm. AmyA and AmyB were very similar with respect to their substrate specificity profiles, clearly preferring amylose over amylopectin, pullulan, and glycogen. Both enzymes also hydrolyzed alpha-, beta-, and gamma-cyclodextrin. Very interestingly, AmyA, but not AmyB, displayed high transglycosylation activity on maltooligosaccharides and also had significant beta-cyclodextrin glycosyltransferase (CGTase) activity. CGTase activity has not been reported for typical alpha-amylases before. The mechanism of cyclodextrin formation by AmyA is unknown.

Adaptation, Physiological↗
PubMed1985

Efficient synthesis and secretion of a thermophilic alpha-amylase by protein-producing Bacillus brevis 47 carrying the Bacillus stearothermophilus amylase gene.

Bacillus subtilis and Bacillus brevis 47-5, carrying the Bacillus stearothermophilus alpha-amylase gene on pUB110 (pBAM101), synthesized the same alpha-amylase as the donor strain as determined by the enzyme's thermal stability and NH2-terminal amino acid sequence. Regardless of the host, the 34-amino acid signal peptide of the enzyme was processed at exactly the same site between two alanine residues. B. brevis 47-5(pBAM101) secreted the enzyme most efficiently of the hosts examined, 100, 15, and 5 times more than B. stearothermophilus, Escherichia coli HB101(pH1301), and B. subtilis 1A289(pBAM101), respectively. The efficient secretion of the enzyme in B. brevis 47-5(pBAM101) was suggested to be due to the unique properties of the cell wall of this organism.

Amino Acid Sequence↗
PubMed1998

[Study on immobilized cells for producing alpha-amylase by using polyving alcohol as the carrier(II): The effect of fermentating conditions on the ability producing alpha-amylase of the cells immobilized with polyving alcohol as the corrier and continuous fermentation of the immobilized cells in CSTR].

The effects of fermentating conditions on the ability of immobilized cells with PVA as carrier for producing alpha-amylase were studied. The continuous fermentation with the immobilized cells were tested in continuous flow stirred tank reactor (CSTR). The results showed that the adaptability of the immobilized Bacillus substilis to pH increased after immobilization. In CSTR, the immobilized cells can be fermentated continuously for 360 hrs and the activity of alpha-amylase can be kept on the level of about 170 u/ml.

Bacillus↗
PubMedDate not supplied

The activity of alpha-amylase and gamma-amylase in serum and pancreatic homogenate of rats with experimental liver damage treated with colchicine.

In connection with extending the therapeutic application of colchicine to include its use in the treatment of liver fibrosis in cirrhosis and possible harmful effects of this drug on other organs, the pancreas in particular, the authors studied this problem experimentally. For this purpose a model of experimental cirrhosis in rats produced with chronic administration of carbon tetrachloride was used, and in the third and ninth months of the experiment the activity of alpha-amylase and gamma-amylase was determined in the serum and pancreatic homogenate. The results did not show any unfavourable effect of colchicine administered in their therapeutic doses for long time periods on the pancreas in experimental rats and in healthy controls.

Animals↗
PubMed1985

Amylase isoenzymes in the acute abdomen: an adjunct in those patients with elevated total amylase.

The role of routine isoamylase determinations in differentiating acute pancreatitis from other causes of an acute abdomen with hyperamylasemia and/or hyperamylasuria was evaluated. Values were analyzed from a control group of 21 patients with acute pancreatitis (group I) and from 100 consecutive patients diagnosed in our emergency department as having an acute abdomen (group II). In group I, 100% of patients had hyperamylasemia, hyperamylasuria, and a P isoamylase fraction greater than 0.75 of the total amylase value. In group II, 50% of patients had hyperamylasemia and/or hyperamylasuria. Of these patients, 44% had a P isoamylase fraction less than 0.75 of the total amylase value, a finding apparently incompatible with a diagnosis of acute pancreatitis as identified by our control group. We conclude that routine isoamylase determinations in patients with an acute abdomen and hyperamylasemia and/or hyperamylasuria allows the differentiation from acute pancreatitis in 44% of cases.

Abdomen, Acute↗
PubMed1987

Crystallization of barley malt alpha-amylases and preliminary x-ray diffraction studies of the high pI isozyme, alpha-amylase 2.

alpha-Amylase isozymes 1 and 2 isolated from germinated barley seeds have been crystallized by the hanging- or sitting-drop vapor diffusion technique. Crystals of alpha-amylase 2 suitable for x-ray diffraction analysis were grown at pH 6.7 and 22 degrees C from a solution of 1 mM calcium chloride, 10 mM MES, and 16% saturated ammonium sulfate. The space group is trigonal P3121 (or P3221) with unit cell dimensions a = b = 135.20 A, c = 79.63 A, and probably two molecules per asymmetric unit.

Crystallization↗
PubMed1979

Specificity of serum amylase and amylase creatinine clearance ratio in the diagnosis of acute and chronic pancreatitis.

In 31 patients with pancreatitis, the amylase to creatinine clearance ratio (CACR) was significantly greater than for controls (10.7 +/- 1.7 vs. 2.6 +/- 0.3, P less than .001). Sixteen pancreatitis patients with serum amylase (SAm) within the normal range had a mean CACR significantly greater than that of 19 hospital control patients with normal SAm (9.2 +/- 1.5 vs. 3.0 +/- 0.4, P less than .001). For control patients a highly significant inverse correlation between SAm and CACR was observed. No relationship was detected between these parameters for pancreatitis patients. The results suggest that the CACR may be of aid in establishing the diagnosis of pancreatitis even in patients without hyperamylasemia.

Acute Disease↗
PubMed1979

[Lung cancer with elevated amylase activity. One observation with study of amylase's isoenzymes (author's transl)].

Amylase is composed by two isoenzymes groups: pancreatic or salivary type. This last part can be increased in many diseases. A case of lung cancer with elevated amylase activity in blood, urine and pleural fluid is reported in a 74-year-old man. This increase was due to salivary type isoamylases with an unusual component which disappeared by neuraminidase treatment. The significance and the origin of this hyperamylasemia with non pancreatic cancer are discussed.

Adenocarcinoma↗
PubMed1983

Amylase:creatinine clearance ratios, serum amylase, and lipase after operations with cardiopulmonary bypass.

Forty-two adults who underwent cardiac operations were studied prospectively for evidence of clinical or subclinical pancreatitis. Clinically detectable pancreatitis was not seen. Serum amylase and lipase levels did not change significantly following operation. The amylase:creatinine clearance ratio (ACCR) immediately following operation was abnormally elevated in 31% of the samples obtained, and the mean ACCR increased from 2.08 +/- 1.85% before operation to 6.2% +/- 6.77% (P less than 0.05). An abnormally elevated ACCR was most often associated with a low urine creatinine concentration. The mean urine creatinine level decreased significantly from 78 +/- 53 mg/dl before operation to 38 +/- 49 mg/dl immediately following operation (P less than 0.02), and 73% of the samples obtained at that time had an abnormally low urine creatinine level (P less than 0.01). The abnormalities observed in ACCR and urine creatinine could not be related to any of several variables presumed to reflect the degree of perioperative physiologic stress, nor could they be related to postoperative hemodynamic performance. It was concluded that ACCR rises following cardiac operation because of perioperative changes in renal function, and not as a reflection of subclinical pancreatic injury.

Adult↗
PubMed1977

Biosynthesis of alpha-amylase and protease by Streptomyces olivaceus 142. I. Regulation of alpha-amylase activity.

Streptomyces olivaceus 142 produces amylase in the logarithmic phase of growth of the culture. The synthesis of the enzyme is induced by maltose and starch. In the case of maltose the synthesis is induced by a contaminating compound, probably being a higher than maltose polymer of glucose. The synthesis of amylase is negatively controlled by catabolic repression. The level of the activity of the enzyme depends not only on the biosynthesis but also on it proteolytic degradation.

Amylases↗
PubMed1977

Biosynthesis of a alpha-amylase and protease by Streptomyces olivaceus 142. III. Some aspects of alpha-amylase induction.

The induction of alpha-amylase in Streptomyces olivaceus 142 depends on the phase of growth of culture and the nature of the carbon sources upon which the cells were grown prior to exposure to inducer. The most susceptible to induction are cells from the initial hours of growth and glycerol -- grown cells. Reduction in the susceptibility of cells to alpha-amylase induction is probably a result of catabolic repression.

Amylases↗
PubMed1994

Markers for pancreatic allograft rejection: comparison of serum anodal trypsinogen, serum amylase, serum creatinine and urinary amylase.

Currently, the markers of acute rejection in pancreas allografts are not consistently reliable. The purpose of this study was to evaluate the ability of sAT to predict acute rejection as compared to serum creatinine (sCr), urinary amylase (uAmy) and serum amylase (sAmy). Eleven first-time acute rejection episodes in bladder-drained SPK recipients were studied. All rejection episodes were biopsy-proven (core kidney 9, fine needle kidney 2, fine needle pancreas 5). Sera obtained from days -7 to -1 (pre-treatment), day 0 (start of anti-rejection treatment), and +1 to +7 (post-treatment) periods were analyzed. Peak median sAT and sAmy levels occurred at day 0 compared to day 1 for sCr. uAmy trough levels occurred on days -4, -5 and +2. The difference between pre-treatment levels and those on day 0 were significant for sAT, sAmy and sCr but not for uAmy. Only in the case of sAT was the difference between day 0 levels and post-treatment levels significant. Both sAmy (0.87) and sCr (0.85) demonstrated positive correlation when compared to sAT whereas uAmy demonstrated a weak negative correlation (-0.24). This study confirms that sAT accurately predicts rejection after SPK transplantation.

Amylases↗
PubMed1999

Insecticidal activity of an alpha-amylase inhibitor-like protein resembling a putative precursor of alpha-amylase inhibitor in the common bean, Phaseolus vulgaris L.

alpha-Amylase inhibitor (alphaAI) in the common bean, Phaseolus vulgaris L., protects seeds from insect pests such as the cowpea weevil (Callosobruchus maculatus) and the azuki bean weevil (C. chinensis). Cultivars which lack alphaAI still show resistance to both bruchids. These cultivars have a glycoprotein that reacts with anti-alphaAI-1 antibodies. The glycoprotein with a molecular mass of 29 kDa (Gp29) was purified and the encoding gene was isolated. The primary structure of Gp29 is the same as alpha-amylase inhibitor-like protein (AIL) from which the encoding gene has already been isolated. AIL resembles a putative precursor of alphaAI, even though it does not form the active inhibitor. However, AIL has some inhibitory effect on the growth of C. maculatus but not C. chinensis. The presence of AIL alone is insufficient to explain the bruchid resistance of common bean cultivars lacking alpha-AI. Common bean seeds appear to contain several factors responsible for the bruchid resistance.

Amino Acid Sequence↗
PubMed1978

Studies on the substrate specificity of Taka-amylase A. XIII. Preparation of 6-deoxy-6-iodomaltooligosaccharides and their inhibitory action against Taka-amylase A1.

O-alpha-D-Glucopyranosyl-(1 leads to 4)-O-6-deoxy-6-iodo-alpha-D-glucopyranosyl-(1 leads to 4)-D-glucopyranose (6'-MT), O-alpha-D-glucopyranosyl-(1 leads to 4)-6-deoxy-6-iodo-D-glucopyranose (6-M), and O-6-deoxy-6-iodo-alpha-D-glucopyranosyl-(1 leads to 4)-D-glucopyranose (6'-M) were prepared and their inhibitory action against Taka-amylase A [EC 3.2.1.1, alpha-1, 4-glucan 4-glucanohydrolase, Aspergillus oryzae] was investigated. The inhibitor constants of 6'-MT and 6'-M were 10 mM and 54 mM, respectively, and both inhibitors showed mixed-type inhibition. 6-M scarcely inhibited the enzyme action.

Amylases↗
PubMed1984

A commercially available S-type amylase inhibitor evaluated for determination of amylase isoenzymes in serum.

On evaluation, an S-type alpha-amylase inhibitor from Sigma shows essentially the same performance characteristics as the inhibitor from wheat germ prepared according to O'Donnell and McGeeney (Biochim Biophys Acta 422:159, 1976). This inhibitor is now commercially available; thus any clinical laboratory can perform isoamylase determinations with a simple, fast procedure that is also suitable for emergency situations.

Amylases↗