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PubMed1992

Characterization of an amylase-binding component of Streptococcus gordonii G9B.

The goal of the present study was to begin characterizing the amylase-binding component(s) on the surface of Streptococcus gordonii G9B. Alkali extracts but not phenol-water extracts of this bacterium inhibited 125I-amylase binding to S. gordonii G9B. To identify the bacterial components involved in amylase binding, the alkali extract was subjected to affinity chromatography on amylase-Sepharose. Immunoblotting with a rabbit antiserum against S. gordonii G9B revealed that a 20-kDa streptococcal component was eluted from the amylase-Sepharose with 1% sodium dodecyl sulfate (SDS), 2 M KSCN, or 0.1 M sodium citrate buffer, pH 4.5. Subsequently, the 20-kDa component was prepared from alkali extracts by electroelution from preparative SDS electrophoresis or by gel filtration chromatography. This component was trypsin sensitive, and an antibody raised against it inhibited the binding of 125I-amylase to S. gordonii G9B. Indirect immunofluorescence microscopy and immunogold electron microscopy demonstrated that both bound amylase and the 20-kDa component were localized to the cell division septum on dividing cells or to polar zones on single cells. In addition, exponentially growing bacteria bound more 125I-amylase than stationary-phase cells did. Collectively, these results suggest that a 20-kDa amylase-binding component is present on the surface of the nascent streptococcal cell wall.

Amylases↗
PubMed1970

Presence of binding site for alpha-amylase and of masking protein for this site on mycelial cell wall of Aspergillus oryzae.

Mycelial cell wall of Aspergillus oryzae M-13 grown in an alpha-amylase-forming medium could not bind alpha-amylase (Taka-amylase A, EC 3.2.1.1). However, by treatment with 1.0 n NaOH at 100 C for 30 min, the wall gained the ability to bind alpha-amylase. This phenomenon was caused by removal of a factor (designated as masking factor) which masked the binding site for alpha-amylase. The masking factor was purified as a preparation giving a single peak in both ultracentrifugation (1.6S) and by gel electrophoresis (M(BPB), 1.0). Approximately 20 mug of the purified factor, bound to 10 mg of the alkali-treated mycelial cell wall, prevented the binding of approximately 100 mug of alpha-amylase or released approximately 100 mug of alpha-amylase which previously was bound to the alkali-treated wall. These findings indicate that the factor has much higher affinity than alpha-amylase for the binding site on the mycelial wall. The masking factor was inducibly formed accompanying the secretion of alpha-amylase.

Amylases↗
PubMed1988

Somatostatin inhibits VIP-stimulated amylase release from perifused guinea pig pancreatic acini.

We have examined the direct effect of somatostatin (SRIF) on basal and stimulated amylase release from guinea pig pancreatic acini using the in vitro method of continuous perifusion. The optimal conditions of flow rate, chamber size, acinar cell volume per chamber, and period of secretagogue infusion were defined for the perifusion system. The kinetic profile of amylase release in response to cholecystokinin-octapeptide (CCK-8), vasoactive intestinal peptide (VIP), and SRIF was studied. Under optimal conditions, the acini were found to remain equally responsive to an ED50 dose of CCK-8 (0.5-0.8 nM) for 12 h of perifusion. The duration of amylase response to any given dose of CCK-8, given for the optimal period of 5 min, was 80-100 min. The total amylase released minus the basal release divided by 90 min (delta response) in response to the maximum effective (Maxeff) dose of CCK-8 (100 nM) was 14,667 +/- 1,433 U/l (amounting to a 10-fold increase compared with basal values). When compared with the amount of total delta amylase released in response to the Maxeff dose of CCK, the total amylase released in response to the Maxeff doses of SRIF (1 microM) and VIP (10 nM) was 10-21% and 51-59%, respectively. SRIF (100 nM) significantly decreased VIP- (0.1-1.0 nM) stimulated amylase release by 45-70% in the perifusion method of study but had no significant effect on the CCK-stimulated amylase release. This suggests that the perifusion method can be used for investigating the mechanism of SRIF-mediated inhibition of VIP effects on amylase release in an in vitro system.

Amylases↗
PubMed1988

Starch and glucose oligosaccharides protect salivary-type amylase activity at acid pH.

Salivary-type amylase may significantly contribute to duodenal starch hydrolysis in exocrine pancreatic insufficiency, provided that gastric inactivation does not occur. We investigated the effect of starch and its hydrolytic products, therefore, on salivary amylase activity in vitro at low pH. When incubated at pH 3 in the presence of 1% starch, 56% of the initial activity of amylase purified from saliva remained after 60 min at 37 degrees C compared with only 6% without starch. Similar protection of amylolytic activity was observed using human milk, which also contains a salivary-type amylase. In addition, partially hydrolyzed starch protected salivary amylase activity at pH 3, and purified glucose oligomers ranging in length from two to seven glucose molecules protected amylase in a concentration-dependent manner. Lactose, sucrose, and glucose, however, were ineffective in sparing amylase. Starch protected amylase activity even in the presence of pepsin, and maltotriose conferred striking protection below pH 3. These studies indicate that salivary-type isoamylases are protected in a simulated gastric environment by substrates of amylase as well as its end products of hydrolysis.

Adult↗
PubMed1988

Amylase secretion by parotid glands and pancreas of diabetic rats during feeding.

Parotid and pancreatic amylase secretion into the gastrointestinal tract during feeding was investigated in diabetic rats. In control rats, both parotid and pancreatic amylase activity decreased after feeding, while the amylase activity present in the gastric and small intestinal contents increased. In diabetic rats, parotid amylase activity, although reduced from control levels, decreased after feeding, and amylase activity of the parotid type appeared in the gastric content. Amylase activities in the diabetic pancreas and small intestinal contents at fasting were markedly reduced and did not show appreciable change with feeding. The total amylase activity in the small intestinal contents after feeding was markedly reduced in the diabetic rats, whereas the ratio of parotid to pancreatic amylase was markedly increased. These results suggest that the amylase secreted from the parotid glands into the gastrointestinal tract during feeding acts not only in the mouth and stomach but also in the small intestine of diabetic rats.

Amylases↗
PubMed1989

Effects of islet hormones on amylase secretion and localization of somatostatin binding sites.

The interaction of insulin and somatostatin on amylase secretion was examined in the isolated perfused rat pancreas. Exogenous insulin (10 mU/ml) significantly potentiated cholecystokinin- (CCK; 0.5 mU/ml) stimulated amylase secretion (12.47 +/- 2.9 micrograms/ml, n = 7). Glucose (16.7 mM) stimulated endogenous insulin secretion (523 +/- 66 microU/ml) and also significantly enhanced CCK-stimulated amylase secretion (13.41 +/- 2.8 micrograms/ml, n = 11). When somatostatin was included in the perfusion media, containing insulin and CCK, amylase secretion was reduced to 3.17 +/- 0.83 micrograms/ml (n = 7), a level comparable to that of CCK-stimulated amylase secretion alone. Similarly, addition of exogenous somatostatin to perfusion media, containing 16.7 mM glucose and CCK, reduced amylase secretion to 4.29 +/- 1.09 micrograms/ml (n = 9). The effect of somatostatin and insulin on carbamylcholine-stimulated amylase secretion was also examined. Exogenous insulin (50 mU/ml) potentiated carbamylcholine- (10(-8) M) stimulated amylase secretion, and addition of exogenous somatostatin to the media containing both insulin and carbamylcholine suppressed the insulin potentiation. Uptake of 125I-[Tyr11]somatostatin in the perfused pancreas was saturable as it decreased significantly with the addition of excess unlabeled somatostatin. Autoradiograms revealed uptake of the ligand by both the endocrine islets and the exocrine pancreas with the highest density of grains observed over the acini. These results support the hypothesis that islet peptides modulate the exocrine pancreas, that somatostatin inhibits amylase secretion by inhibiting the action of insulin, and that somatostatin may act directly on the exocrine pancreas via specific receptors on acinar cells.

Amylases↗
PubMed1990

Effects of diabetes and insulin on alpha-amylase messenger RNA levels in rat parotid glands.

Previous studies have shown that amylase levels are reduced significantly in the pancreas and parotid gland of diabetic rats and that insulin reverses this effect and increases the secretory protein levels. In the pancreas, these changes in amylase protein levels are accompanied by parallel changes in amylase mRNA levels. In the present study, the effects of diabetes and subsequent insulin treatments on contents (per cell) of amylase protein and its mRNA in parotid glands were compared in rats rendered diabetic with an injection of a beta-cell toxin, streptozotocin (STZ). Both amylase protein and its mRNA contents were reduced significantly in diabetic rats, compared with control rats, and this reduction was reversed following insulin injections of diabetic rats. In insulin-injected diabetic rats, amylase protein contents increased before a detectable increase in amylase mRNA levels was seen. The mRNA contents of a non-secretory protein, actin, did not change during diabetogenesis or subsequent insulin treatments. The reductions in parotid contents of amylase and its mRNA in diabetic rats and the reversal of these changes by insulin are similar to those changes that occur in the pancreas under the same conditions. However, the magnitude of these changes in parotid glands was much smaller than in the pancreas, and the effect of insulin on amylase mRNA synthesis was not as immediate as in the latter gland.

Actins↗
PubMed1994

Emergence in human dental plaque and host distribution of amylase-binding streptococci.

Salivary amylase is known to bind specifically to several species of oral streptococci. To assess the importance of this interaction in bacterial colonization of the oral cavity, we determined the proportion and identity of amylase-binding bacteria (ABB) in dental plaque of humans and various salivary amylase-secreting and non-secreting mammalian species. The numbers of ABB in undisturbed plaque collected over time from tooth surfaces of six human volunteers or from 14 other mammalian species were determined by means of a replicating assay. The mean proportion of ABB cultured aerobically from human teeth at 2 h was 10.5% (SD 10), at 8 h 7.9% (8), at 24 h 13% (11), and at 48 h 12% (9). The mean proportion of anaerobically cultured ABB found at 2 h was 3% (SD 4), at 8 h 5% (5), at 24 h 12% (9), and at 48 h 16% (12). Amylase-binding bacteria cultured from these samples resembled Streptococcus mitis, Streptococcus gordonii, Streptococcus salivarius, Streptococcus crista, or unidentified streptococci. In addition, only animals exhibiting salivary amylase activity in their saliva harbored ABB (ranging from 2 to 31% of the total flora), with the exception of the pig, where no ABB were found to colonize, despite considerable amylase activity in saliva. Only strains resembling S. mitis and S. salivarius and unspeciated strains were isolated from these mammals. These results suggest that amylase-binding streptococci are the predominant ABB in human plaque, and their numbers generally increase as plaque develops. Since ABB colonized only the oral cavities of hosts demonstrating salivary amylase activity, the ability to bind amylase may play an important role in oral colonization by these bacteria.

Amylases↗
PubMed1999

Relationship between parotid amylase secretion and osmolality in the gastric contents of rats fed a pelleted or liquid diet.

The relationship between parotid amylase secretion and the osmolality in the gastric contents of rats fed a pelleted or liquid diet was investigated. In sham-operated rats fed a pelleted diet, amylase activity in the parotid glands decreased, amylase activity in the plasma increased, and there was strong amylase activity in the gastric contents. As a result, both reducing sugar concentration and osmolality in the gastric contents increased. In parotid duct-ligated rats, the feeding of a pelleted diet affected neither parotid nor plasma amylase activity and there was little amylase activity in the gastric contents; this resulted in decreased starch digestion. The amylase activity in the gastric contents of rats fed a liquid diet was lower than that of rats fed the pelleted diet. Both the reducing sugar concentration and osmolality in the gastric contents of rats fed the liquid diet were lower than those of rats fed the pelleted diet. However, both the reducing sugar concentration and osmolality in the gastric contents of rats fed the liquid diet were higher than those in the liquid diet itself. A small quantity of parotid amylase seems to effectively digest a large part of the starch in the stomaches of rats fed the liquid diet. These findings suggest that amylase secreted from parotid glands increases osmolality in the gastric contents via the production of reducing sugars from starch in rats when fed either pelleted or liquid diets.

Amylases↗
PubMed2001

Mecamylamine, a nicotinic receptor channel antagonist, affects amylase secretion by isolated pancreatic acinar cells.

It is well established that CCK is a potent stimulator of amylase secretion from the pancreatic acinar cells, while nicotine is an effective inhibitor of such secretion. The present study was conducted to determine whether mecamylamine, a well-established ganglionic blocker drug, could influence amylase secretion from the pancreas. Male Sprague-Dawley rats were fasted, sacrificed, the pancreas removed, and pancreatic acinar cells isolated and purified. The cells were equally divided into 4 different flasks and treated with the following solutions: (control), 10 mM nicotine, 10 microM mecamylamine or 100 microM mecamylamine. The cells were washed twice after 30 min incubation at 37 degrees C, resuspended in HR buffer, and amylase release in response to graded doses of CCK-8 was measured in cells from each flask. The study was repeated four times. Basal amylase release was not different by treatment with nicotine or different doses of mecamylamine. In response to CCK-8, amylase release was decreased by nicotine and by mecamylamine (100 microM) when compared with control. Amylase release was similar between control and mecamylamine (10 microM). Peak amylase released with the maximal dose of CCK-8 (1 x 10(-10) M) was less in cells treated with nicotine when compared with those measured cells treated with saline or with the two doses of mecamylamine. The release of amylase was suppressed in a similar manner in all treatment groups in response to supramaximal (3 x 10(-10) to 1 x 10(-9) M) doses of CCK-8. Mecamylamine, at the high dose, acts on isolated pancreatic acinar cells to decrease amylase release in a manner similar to that found with nicotine. Both of these drugs, nicotine and mecamylamine, may act via CCK receptors via two different intracellular mechanisms.

Amylases↗
PubMed1990

Renal handling of amylase and immunoreactive trypsin in pancreatic cancer and chronic pancreatitis.

In order to evaluate the renal metabolism of amylase and immunoreactive trypsin (IRT) in chronic pancreatic disease, we assayed amylase, IRT and creatinine in serum and urine and gamma-glutamyl transferase (GGT) in dialyzed urine as well as alpha-glucosidase (AGL) and ribonuclease (RNase) in 24 control subjects, 34 patients with pancreatic cancer, 52 with chronic pancreatitis and 32 with extra-pancreatic diseases. Urinary amylase and IRT outputs were found to be more elevated in chronic pancreatitis than in control subjects. The levels of serum amylase, its renal inputs and outputs were correlated with the corresponding IRT values. Multiple regression analyses (dependent on amylase or IRT urinary outputs, circulating levels of the two enzymes, creatinine clearance and the excretion of GGT, AGL and RNase predictor variables) showed significant correlations. The standardized partial regression coefficients found to be significant were: GGT, RNase and serum amylase for amylase, and GGT and RNase for IRT. No difference was found between amylase and IRT outputs in patients with chronic pancreatitis, taking the presence or the absence of alcohol abuse, exocrine insufficiency and pancreatic pseudocysts into consideration. Urinary GGT excretion correlated with serum amylase and IRT levels.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed2006

[Expression of a thermostable a-amylase mutant into Escherichia coli and Pichia pastoris].

Alpha-amylase are of considerable commercial value. It can be produced by a wide variety of microorganisma. The alpha-amylase gene (amyE) from Bacillus licheniformis, which is widely used for the industrial hydrolysis of starch, was mutated (amyEM), then amplified by PCR and inserted into pBV220 and pPIC9k to obtain the recombinant vector pBV220-amyEM and pPIC9k-amyEM. These recombinant vectors were transformed into corresponding competent cell E. coli DH5alpha and P. pastoris GS115 respectively. The resulting recombinant strains, DH5alpha/pBV220-amyEM and GS115/ pPIC9k-amyEM, were then screened by measuring the enzymatic activity and SDS-PAGE. DH5alpha/pBV220-amyEM was induced by temperature and GS115/pPIC9k-amyEM by methanol. In contrast to the parent cells, the a-amylases were expressed in both the recombinant strains. In E. coli the molecular weight was approximately 55kDa; optimal temperature and pH of the recombinant a-amylase were 80 degrees C - 90 degrees C and 6.0 respectively. The recombinant amylase had high activity in pH 5.0 - 5.5 compared to wild type. In Pichia pastoris, the recombinant amylase was secreted to the medium; molecular weight was 60kDa for the putative post-translational modifications; optimal pH shifted to 5.5. The specific activities of alpha-amylase produced by E. coli and P. pastoris were 8.1U/mg and 102U/mg respectively. This result indicated that the alpha-amylase were secreted into the culture medium with high efficiency in the recombinant P. pastoris High activity in high temperature and lower pH properties impart the recombinant amylase potential applications in industry.

Escherichia coli↗
PubMed1990

[Studies of the manifold of amylase].

alpha-Amylase (1.4-alpha-D-glucan-glucanohydrolase, E.C 3.2.1.1) is distributed widely in animal and plant kingdoms. A number of properties of this enzyme have been recognized molecular biologically using animal organs. On the other hand, physiological roles and specificities of serum amylase are not known. The source organs of serum amylase have not been confirmed in every animal. The purposes of the experiments are to find out the specificities and varieties of amylase in some kinds of animals. The following results were obtained. 1. Amylase activities in the sera (body fluids) of some animals (Mammals, Birds, Amphibians, Fishes, Insects and Shellfish, 25 kinds altogether) were quite different from each other. The highest amylase activity except insects was observed in the serum of hamster (400 units) and the lowest was in the serum of horse (0.4 units). The activity of locust and oriental longheaded locust, eating grain mainly, was high (locust, 1965 units). 2. Five isoamylases were detected in the serum of rat. Four of them migrated to anode. 2-5 isoamylases were observed in other subjects and the mobility of isoamylases was different from each other. This seemed to be caused by the differences of isoamylase proteins. 3. Amylase activities in the brain, parotid gland, submandibular gland, sublingual gland, tongue, lung, heart, liver, stomach, spleen, pancreas, adrenal, serum and urine of hamster, rat, mouse and rabbit were measured. The activity was especially high in the parotid gland and pancreas. In rabbit, however, amylase activity in these organs was lower than that of other animals. 4. Isoamylases in some organs of four kinds of animals (hamster, rat, mouse and rabbit) were separated electrophoretically. Isoamylases in the serum of rat, hamster and mouse were similar to those in the parotid, submandibular and sublingual glands, respectively. In rabbit, it was difficult to separate isoamylases in the parotid gland and pancreas. 5. Amylases in the parotid gland and locus body were purified by column chromatography (potato starch).

Amphibians↗
PubMed1991

[Alpha-amylase isoenzymes in serum and saliva of patients with anorexia and bulimia nervosa].

In the serum and saliva of 45 patients with eating disorders and in 30 normal controls, alpha-amylase activity and isoamylase levels were measured. Of the 45 patients evaluated, 12 had restrictive anorexia nervosa, 13 were bulimic anorectics and 20 had bulimia nervosa. In all these groups, the mean alpha-amylase values in serum and saliva were higher than that of the control group. The proportion of pancreatic (P)- and salivary (S)-alpha-amylase isoenzymes in serum were within the normal range for the patient group with restrictive anorexia nervosa, whereas the bulimic anorexia nervosa and bulimia nervosa patients showed significantly greater increases in S- than P-isoamylase activity. The correlation of the salivary alpha-Amylase isoenzym pattern in serum and saliva pointed to the salivary glands as origin of the elevated salivary isoamylase levels in serum. Hyperamylasemia was found in 10 (25%) of the 45 patients with eating disorders. Three of these patients showed besides an increased S-alpha-amylase activity also pathologically elevated P-alpha-amylase and lipase activity in serum; however there were no abdominal symptoms, laboratory data or ultrasonic signs of pancreatitis. In all patients with eating disorders, the mean concentration and secretion of alpha-amylase in saliva were increased. Swelling of the salivary glands was present in 14 patients. In these cases the percentage of salivary-isoamylase activity in total serum alpha-amylase activity was increased significantly, whereas the alpha-amylase secretion in the resting saliva was decreased.

Adolescent↗
PubMed1986

Amylase levels in semen and saliva stains.

Amylase levels were determined for 148 semen samples and 20 saliva samples as well as for their corresponding stains. The effect of aging on the detectability of amylase activity in these stains was also investigated. The Phadebas amylase test was used for the quantitative assay of amylase. High levels of amylase in fluid saliva resulted in high levels being detected in saliva stains. Lower levels present in most seminal fluids produce little or no detectable amounts of amylase in stains. Interpretations are made as to the possible sources of amylase activity found in stains from laboratory casework based on both the amylase concentration and the elapsed time between collection and analysis. The evidential value of the presence or absence of amylase activity in casework stains is also discussed.

Amylases↗
PubMed1987

Metal binding characteristics of human salivary and porcine pancreatic amylase.

With the exception of calcium very little is known about metal binding characteristics of either human salivary or porcine pancreatic amylase. In order to learn more about these protein-metal binding interactions, calcium-free human salivary and porcine pancreatic amylase [P(protein)] were obtained by carboxymethylcellulose chromatography of the partially purified proteins. Because these proteins acquired small amounts of calcium after further preparatory studies, they were dialyzed against 1 mM EDTA, pH 7.4, at 22 degrees C, which removed essentially all acquired calcium. The calcium-free amylases were then subjected to equilibrium dialysis against copper or zinc solutions with or without added glycine. The experimental data were fitted to appropriate mathematical equations, and binding constants of the metal complexes were calculated. Both human salivary and porcine pancreatic amylase were found to have two metal ion binding sites, only one of which was selective for calcium. Copper or zinc appeared to bind to the second site forming the species CuCaLP (or ZnCaP), where L, a ligand, is the glycine anion. Neither copper nor zinc displaced calcium from human salivary amylase, although copper bound to both binding sites in human salivary apoamylase to form the species Cu2L2P in which the amylase molecule appeared to form a bridge between the two copper atoms. In the case of the zinc-human salivary apoamylase system, the experimental data could not be analyzed quantitatively since the protein formed an insoluble complex species. Copper displaced calcium from porcine pancreatic amylase and formed a mixed ligand species similar to that formed with human salivary apoamylase. Zinc bound to both metal binding sites of porcine pancreatic apoamylase, forming species ZnP and Zn2P, although it did not displace calcium from the protein. While calcium in amylase is known to be critical for its amylolytic activity, little is known about the function of either zinc or copper in amylase albeit both of these metals are important in biological systems.

Amylases↗
PubMed1988

Renal clearance of pancreatic and salivary amylase relative to creatinine clearance in patients with renal disease and proteinuria.

To study the charge-selective properties of the glomerular filter in renal disease, we measured the fractional clearance, relative to creatinine clearance (ECC), of the amylase isoenzymes pancreatic amylase and salivary amylase, which have identical size but different charge. In 63 healthy subjects the mean (and SD) fractional excretion of pancreatic amylase, 4.07% (1.24%), was fourfold that of salivary amylase: 1.02% (0.54%). For 29 patients with renal disease and proteinuria, the mean fractional excretion of pancreatic amylase was significantly lower, 3.31% (1.94%), and that of salivary amylase significantly higher, 2.06% (1.41%), than in controls. In these patients, fractional excretions of both these isoenzymes were negatively correlated with urinary excretion of beta 2-microglobulin and ECC. Evidently, differences in clearances of pancreatic and salivary amylase are a consequence of differences in charge-related glomerular filtration. The relative increase of salivary amylase clearance in patients with renal disease and proteinuria is most probably caused by a loss of the charge-selective properties of the glomerular basement membrane.

Adult↗
PubMed1989

Immunocatalytic assay of pancreatic alpha-amylase in serum and urine with a specific monoclonal antibody.

In this immunocatalytic assay for alpha-amylase (EC 3.2.1.1) of pancreatic origin, a highly specific monoclonal antibody coupled to plastic beads is used to extract pancreatic amylase from samples, leaving salivary amylase in solution. The catalytic activity of the bound pancreatic amylase is then determined with blocked p-nitrophenyl maltoheptaoside as substrate. The method shows no cross-reactivity with salivary amylase, analytical recovery is 89-109% for pancreatic amylase, and interassay imprecision is 7.1-7.7%. We used the method to determine pancreatic amylase in serum and urine from healthy controls and different patient groups. The reference intervals for 34 supposedly healthy controls were: serum, 10-48 U/L (mean 27 U/L); urine, less than 20-435 U/L (mean 104 U/L). Results by the present assay correlated well with a salivary amylase inhibition assay (Boehringer Mannheim). We conclude that the described immunocatalytic assay is clinically useful for detecting increased activities of pancreatic amylase in serum and urine.

Acute Disease↗