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PubMed2005

Inhibitory specificity and insecticidal selectivity of alpha-amylase inhibitor from Phaseolus vulgaris.

The primary structure and proteolytic processing of the alpha-amylase isoinhibitor alpha AI-1 from common bean (Phaseolus vulgaris cv. Magna) was determined by protein chemistry techniques. The inhibitory specificity of alphaAI-1 was screened with a panel of the digestive alpha-amylases from 30 species of insects, mites, gastropod, annelid worm, nematode and fungal phytopathogens with a focus on agricultural pests and important model species. This in vitro analysis showed a selective inhibition of alpha-amylases from three orders of insect (Coleoptera, Hymenoptera and Diptera) and an inhibition of alpha-amylases of the annelid worm. The inhibitory potential of alphaAI-1 against several alpha-amylases was found to be modulated by pH. To understand how alphaAI-1 discriminates among closely related alpha-amylases, the sequences of the alpha-amylases sensitive, respectively, insensitive to alphaAI-1 were compared, and the critical determinants were localized on the spatial alpha-amylase model. Based on the in vitro analysis of the inhibitory specificity of alphaAI-1, the in vivo activity of the ingested alphaAI-1 was demonstrated by suppression of the development of the insect larvae that expressed the sensitive digestive alpha-amylases. The first comprehensive mapping of alphaAI-1 specificity significantly broadens the spectrum of targets that can be regulated by alpha-amylase inhibitors of plant origin, and points to potential application of these protein insecticides in plant biotechnologies.

Amino Acid Sequence↗
PubMed2004

Posttranscriptional regulation of alpha-amylase II-4 expression by gibberellin in germinating rice seeds.

Hormonal regulation of expression of alpha-amylase II-4 that lacks the gibberellin-response cis-element (GARE) in the promoter region of the gene was studied in germinating rice (Oryza sativa L.) seeds. Temporal and spatial expression of alpha-amylase II-4 in the aleurone layer were essentially identical to those of alpha-amylase I-1 whose gene contains GARE, although these were distinguishable in the embryo tissues at the early stage of germination. The gibberellin-responsible expression of alpha-amylase II-4 was also similar to that of alpha-amylase I-1. However, the level of alpha-amylase II-4 mRNA was not increased by gibberellin, indicating that the transcriptional enhancement of alpha-amylase II-4 expression did not occur in the aleurone. Gibberellin stimulated the accumulation of 45Ca2+ into the intracellular secretory membrane system. In addition, several inhibitors for Ca2+ signaling, such as EGTA, neomycin, ruthenium red (RuR), and W-7 prevented the gibberellin-induced expression of alpha-amylase II-4 effectively. While the gibberellin-induced expression of alpha-amylase II-4 occurred normally in the aleurone layer of a rice dwarf mutant d1 which is defective in the alpha subunit of the heterotrimeric G protein. Based on these results, it was concluded that the posttranscriptional regulation of alpha-amylase II-4 expression by gibberellin operates in the aleurone layer of germinating rice seed, which is mediated by Ca2+ but not the G protein.

Base Sequence↗
PubMed2002

Differences in the regulatory mechanism of amylase release by rat parotid and submandibular glands.

It is not known whether the mechanisms involved in amylase release in submandibular and parotid glands are similar. Here, the participation of different signalling pathways in amylase release by the parotid and submandibular glands of the male rat was compared by studying the secretory response after beta-adrenergic stimulation. The beta-adrenergic agonist isoproterenol induced an increase of cAMP in both salivary glands, but while in the parotid it triggered amylase release, in the submandibular it was unable to increase amylase secretion. Parotid amylase release was dependent on adenylate cyclase activation, as SQ-22536 inhibited the secretory effect. In contrast, submandibular amylase secretion did not depend on the intracellular concentration of cAMP, as SQ-22536 did not modify its secretory response. Moreover, other activators of adenylate cyclase, such as forskolin and prostaglandin E2, also failed to modify amylase release by the submandibular gland. Neither ionophores nor calcium-blocking agents, as well as calcium-calmodulin and nitric oxide synthase inhibitors, were effective in modifying basal amylase release by the submandibular gland. However, the disruption of microfilaments with cytochalasin B, but not the disruption of microtubules with colchicine, prevented amylase release in that gland. It is concluded that amylase exocytosis in the submandibular gland is a constitutive non-regulated phenomenon, as it is independent of extracellular or intracellular signals. It depends only on the integrity of the microfilaments, probably used by the vesicles to travel from the Golgi apparatus to the plasma membrane.

Actin Cytoskeleton↗
PubMed1990

Structural relationship between the enzymatic and streptococcal binding sites of human salivary alpha-amylase.

Previous studies have demonstrated that human salivary alpha-amylase specifically binds to the oral bacterium Streptococcus gordonii. This interaction is inhibited by substrates such as starch and maltotriose suggesting that bacterial binding may involve the enzymatic site of amylase. Experiments were performed to determine if amylase bound to the bacterial surface possessed enzymatic activity. It was found that over one-half of the bound amylase was enzymatically active. In addition, bacterial-bound amylase hydrolyzed starch to glucose which was then metabolized to lactic acid by the bacteria. In further studies, the role of amylase's histidine residues in streptococcal binding and enzymatic function was assessed after their selective modification with diethyl pyrocarbonate. DEP-modified amylase showed a marked reduction in both enzymatic and streptococcal binding activities. These effects were diminished when DEP modification occurred in the presence of maltotriose. DEP-modified amylase had a significantly altered secondary structure when compared with native enzyme or amylase modified in the presence of maltotriose. Collectively, these results suggest that human salivary alpha-amylase may possess multiple sites for bacterial binding and enzymatic activity which share structural similarities.

Acids↗
PubMed2001

Endogenous cholecystokinin plays a role in down-regulation of pancreatic amylase independent of dietary carbohydrate in rats.

The role of cholecystokinin (CCK) in the regulation of pancreatic amylase has not been fully clarified. We examined the effects of hyperCCKemia with chronic pancreatico-biliary diversion (PBD) and blockade of CCK(A)-receptor on rat pancreatic amylase activity and mRNA abundance. Also, we examined the relationship between diet and CCK in terms of regulation of pancreatic amylase. PBD was produced by transposition of the duodenal segment containing the ampulla of Vater to the upper ileum. A potent CCK(A)-receptor antagonist, devazepide, was injected (6 mg/kg body weight per day for 5 days) in the PBD rats fed with diets containing normal or low level of carbohydrate (695 or 345 g sucrose/kg diet). The specific activity and mRNA abundance of the pancreatic amylase were constantly lower 4, 10 and 28 days after PBD than those after the sham operation. Devazepide treatment completely restored the amylase activity lowered by PBD without any increases in amylase mRNA. Feeding a high-protein low-carbohydrate diet suppressed the pancreatic amylase activity and mRNA abundance in PBD rats to a similar degree in those treated, and those untreated, with devazepide. We conclude that endogenous CCK suppresses pancreatic amylase production, and we speculate that CCK reduced translational efficiency of amylase mRNA. The effect of CCK on amylase production is independent of regulation by dietary carbohydrate.

Amylases↗
PubMed2003

Flow-injection-type biosensor system for salivary amylase activity.

The authors aim to establish a method that can quantitatively evaluate vital reactions to stress. We have been examining the correlation between stress and salivary amylase activity in order to verify its validity as a stress index. In order to quantify human stress, which changes over time, the relationship between stress and salivary amylase activity must be verified by fast and repeated analysis of salivary amylase activity. Standard biosensors are designed such that the enzyme immobilized on an electrode (enzyme electrode) and the substrate-dependent activity is measured. The reverse approach of measuring the alpha-amylase-dependent activity was adopted. We fabricated an amylase activity analytical system. Maltopentaose was selected as a substrate for alpha-amylase and a flow-injection-type device was used to supply maltopentaose continuously. alpha-Glucosidase, having relatively low enzyme activity, was immobilized on a pre-activated membrane so that it could be enclosed in a pre-column, Glucose oxidase, having higher enzyme activity, was immobilized on a working electrode so that it could function as an amperometric biosensor. A saliva-collecting device was fabricated to make saliva pretreatment unnecessary. As a result, an amylase activity analytical system was fabricated that enabled us to measure salivary amylase activity from 0 to 30 kU/l, with an R(2) value of 0.97. The time-course changes in the salivary amylase activities for 1 week were 5.1%, and the initial sensitivity remained nearly constant. Through this study, we were able to verify the possible development of the amylase activity analytical system.

Amylases↗
PubMed2002

Pyrococcus furiosus alpha-amylase is stabilized by calcium and zinc.

The hyperthermophilic archeon Pyrococcus furiosus produces an extracellular alpha-amylase that belongs to glycosyl hydrolases' family 13. This enzyme is more thermostable than its bacterial and archaeal homologues (e.g., Bacillus licheniformis TAKA-term and Pyrococcus kodakaraensis KOD1 alpha-amylases, respectively) even without adding Ca(2+) ions. Unlike the TAKA-therm amylase that contains no cysteine, the P. furiosus enzyme contains five cysteines (C152, C153, C165, C387, and C430), only four of which (C152, C153, C387, and C430) are conserved in the P. kodakaraensis alpha-amylase. To test the potential function of cysteines in P. furiosus alpha-amylase stability, these five residues were substituted with Ser or Ala-either one-by-one or in sequence-to produce eight mutant enzymes. Mutation C165S dramatically destabilized P. furiosus alpha-amylase. At the same time, the quadruple mutant enzyme C152S/C153S/C387S/C430A (mutant SSCSA) was as thermostable as the wild-type enzyme. Mutant SSCSA and wild-type alpha-amylases were strongly destabilized by dithiothreitol and ethylenediaminetetraacetic acid, suggesting that metal binding can be involved in this enzyme's thermostability. Inductively coupled plasma-atomic emission spectrometry showed the presence of Ca(2+) and Zn(2+) metal ions in P. furiosus alpha-amylase. Although Ca(2+) is known to contribute to alpha-amylase's stability, the absence of two out of the three conserved Ca(2+) ligands in the P. furiosus enzyme suggests that a different set of amino acids is involved in this enzyme's Ca(2+) binding. We also provide evidence suggesting that Cys165 is involved in Zn(2+) binding and that Cys165 is essential for the stability of P. furiosus alpha-amylase at very high temperatures.

Amino Acid Substitution↗
PubMed2005

Interactions of alpha-amylase and calcium chelator during neutral detergent fiber analysis.

Amylase and calcium chelators, such as disodium ethylene diaminotetraacetate (EDTA), are used in analysis of neutral detergent fiber (NDF) to dissolve starch and pectin, respectively. However, these reagents may interfere with each other's activity. Six combinations of alpha-amylase and EDTA were examined for determining NDF values of beet pulp (Beta vulgaris), ground corn (Zea mays L.), timothy hay (Phleum pratense), and soybean meal (Glycine max L). For treatment A, 2.5 mL of alpha-amylase was added 5 min after boiling. Other treatments differed as follows: (B) 4.5 mL of alpha-amylase, (C) 4.5 mL of alpha-amylase added 30 min after boiling, (D) delayed addition of EDTA to 30 min after boiling, (E) no EDTA, and (F) no alpha-amylase. Inclusion of EDTA interfered with amylase activity in corn grain samples, and addition of amylase to beet pulp and soybean meal samples reduced the effectiveness of EDTA and increased ash in the NDF residue. Amylase should not be used for samples that do not contain starch. Calculating NDF on an ash-free basis minimized the negative effects of amylase on EDTA activity.

Beta vulgaris↗
PubMed1986

Insulin resistance is accompanied by impairment of amylase-gene expression in the exocrine pancreas of the obese Zucker rat.

Insulin plays a major role in the control of pancreatic amylase biosynthesis. In this study we determined glucose metabolism by pancreatic acini as well as the pancreatic content of both amylase protein and amylase mRNA during development of insulin resistance in the obese Zucker rat. At age 4 weeks there were no abnormalities detected in the above parameters, although the obese animals were already hyperinsulinaemic. At 6 weeks glucose metabolism was decreased by 50% in acini from obese rats, whereas pancreatic amylase-gene expression was only slightly impaired. At 22 weeks glucose metabolism was decreased by 50%, amylase content by 55% and amylase mRNA by 60% in acinar tissue of obese rats. As expected, hyperinsulinaemia increased markedly with age. Thus development of severe insulin resistance was associated with impairment of amylase-gene expression. To decrease insulin resistance, one group of adult obese rats was treated with Ciglitazone for 4 weeks. A lowered plasma insulin concentration without alteration of food intake was taken as evidence of decreased insulin resistance. This was associated with normalization of glucose metabolism and a marked increase of both amylase content of pancreatic tissue and amylase mRNA. In conclusion, both the increase of insulin resistance with age and its partial reversal by Ciglitazone treatment appear to modulate pancreatic amylase-gene expression in the obese Zucker rat.

Amylases↗
PubMed1997

Expression, secretion, and processing of rice alpha-amylase in the yeast Yarrowia lipolytica.

The gene encoding rice alpha-amylase in Oryza sativa was expressed in the yeast Yarrowia lipolytica, which is a potential host system for heterologous protein expression. For efficient secretion, the strong and inducible XPR2 promoter was used in the construction of four kinds of expression vectors with the following configurations between the XPR2 promoter and terminator: 1) XPR2 prepro-region-rice alpha-amylase coding sequence, 2) rice alpha-amylase signal peptide-rice alpha-amylase coding sequence, 3) XPR2 signal peptide-rice alpha-amylase coding sequence, and 4) XPR2 signal peptide-dipeptide stretch-rice alpha-amylase coding sequence. Secretion of active recombinant rice alpha-amylase into the culture medium was achieved only in the first two cases, demonstrating that the XPR2 signal peptide is not sufficient to direct the secretion of heterologous protein. Furthermore, our study shows that the XPR2 prepro-region causes imprecise processing (after Pro150-Ala151 or Val135-Leu136 instead of Lys156-Arg157) and leads to N-terminal amino acid sequences that differ from that of native rice alpha-amylase. Secondary structure analysis proposed that the structural form in the vicinity of the KEX2-like endopeptidase processing site in the XPR2 pro-region might play a critical role in the processing of heterologous proteins. These results suggest that the XPR2 pro-region is dispensable for obtaining the precise N-terminal amino acid in heterologous protein secretion. In contrast, utilizing the rice alpha-amylase signal peptide was sufficient in directing secretion of recombinant protein with the expected N-terminal sequence, indicating that the signal peptide of rice alpha-amylase was effectively recognized and processed by the Y. lipolytica secretory pathway.

Cloning, Molecular↗
PubMed2003

Structural and enzymatic analysis of soybean beta-amylase mutants with increased pH optimum.

Comparison of the architecture around the active site of soybean beta-amylase and Bacillus cereus beta-amylase showed that the hydrogen bond networks (Glu380-(Lys295-Met51) and Glu380-Asn340-Glu178) in soybean beta-amylase around the base catalytic residue, Glu380, seem to contribute to the lower pH optimum of soybean beta-amylase. To convert the pH optimum of soybean beta-amylase (pH 5.4) to that of the bacterial type enzyme (pH 6.7), three mutants of soybean beta-amylase, M51T, E178Y, and N340T, were constructed such that the hydrogen bond networks were removed by site-directed mutagenesis. The kinetic analysis showed that the pH optimum of all mutants shifted dramatically to a neutral pH (range, from 5.4 to 6.0-6.6). The Km values of the mutants were almost the same as that of soybean beta-amylase except in the case of M51T, while the Vmax values of all mutants were low compared with that of soybean beta-amylase. The crystal structure analysis of the wild type-maltose and mutant-maltose complexes showed that the direct hydrogen bond between Glu380 and Asn340 was completely disrupted in the mutants M51T, E178Y, and N340T. In the case of M51T, the hydrogen bond between Glu380 and Lys295 was also disrupted. These results indicated that the reduced pKa value of Glu380 is stabilized by the hydrogen bond network and is responsible for the lower pH optimum of soybean beta-amylase compared with that of the bacterial beta-amylase.

Bacillus cereus↗
PubMed1993

Total serum amylase but not lipase correlates with measured glomerular filtration rate.

Elevated serum amylase and lipase levels have been reported in patients with renal failure. Because the diagnosis of pancreatitis is often based on elevations in serum amylase or lipase along with abdominal pain, we determined the relationship between total serum amylase, lipase, and glomerular filtration rate (GFR). Thirty-three subjects, 13 men and 20 women (age range, 21-79), were included in the study. There was a statistically significant correlation between serum amylase and the actual GFR (r = -0.43, p = 0.01). However, no such correlation was seen with lipase. No correlation between total serum amylase and lipase was observed. Three subjects had elevated amylase (240-433 U/L, normal 50-225). Three patients had slightly elevated lipase (29-31 U/dl, normal 8-28). All patients were asymptomatic. Of 11 subjects with GFR < 50 cc/min, only one had an elevated amylase and another an elevated lipase. Our data suggest that although the total serum amylase level is determined in part by the GFR, elevations in either amylase or lipase may not occur even in the presence of renal failure. Therefore, even small elevations in the total serum amylase or lipase in a patient with renal insufficiency may be clinically significant.

Adult↗
PubMed1986

The effect of the inverted repeat structure on the production of the cloned Bacillus amyloliquefaciens alpha-amylase.

An inverted repeat structure from Bacillus natto preceding the Bacillus subtilis alpha-amylase gene has been suggested to be responsible for the enhancement of alpha-amylase production [Yamazaki et al. (1983) J. Bacteriol. 156, 327-337]. A similar inverted repeat region has also been found upstream from the Bacillus amyloliquefaciens alpha-amylase gene and shown to function as a transcription termination signal of an upstream operon of 2.2 X 10(3) bases (2.2 kb) (Kallio et al., following paper in this journal). The removal of this DNA region reduced the level of alpha-amylase production by 70% and led to concomitant formation of a readthrough transcript arising from the promoter of the 2.2-kb operon. To test whether the readthrough transcript affected the alpha-amylase production, the promoter of the 2.2-kb operon was removed from plasmid constructions carrying either intact or deleted inverted repeat sequences. When cultures carrying the above plasmids were assayed for alpha-amylase activity, both constructions produced equal amounts of alpha-amylase. Thus, the inverted repeat structure preceding the alpha-amylase promoter does not, as such, enhance the alpha-amylase production. Instead, its presence prevents the inhibition of alpha-amylase expression caused by the readthrough transcripts from the upstream promoter.

Bacillus↗
PubMed1996

Salivary alpha-amylase as a measure of endogenous adrenergic activity.

This investigation was designed to evaluate the production rates and concentrations of salivary alpha-amylase as a measure of adrenergic activity under several conditions of stress in human subjects. Saliva and blood samples were simultaneously collected from men at four 15 min intervals both before and after regimens for exercise, a written examination, or a rest period. The regressions of salivary alpha-amylase on plasma norepinephrine (NE) concentrations were significant for both exercise (P < 0.001) and examination (P < 0.01) protocols. Aerobic exercise induced a 3-fold mean increase in alpha-amylase; both NE and epinephrine (EP) increased approximately 5-fold over control levels. Levels of alpha-amylase and NE returned to control levels within 30-45 min after exercise, but EP remained elevated by approximately 2-fold during the remaining hour of observation. During the written examination, alpha-amylase and NE, but not EP, concentrations increased in parallel. In further studies the effects of exercise and exposure to heat and cold on the relationship of salivary alpha-amylase to heart rate and body temperature were investigated. Greater intensities of exercise were associated with greater increases in alpha-amylase concentrations. During heat exposure in a sauna (66 degrees C for 40 min) amylase, heart rate and body temperature all increased progressively. However, during exposure to cold (4 degrees C for 40 min) amylase increased rapidly, though heart rate and body temperature remained unchanged. Salivary cortisol concentrations were unchanged during exposure to heat or cold. We conclude that salivary alpha-amylase concentrations are predictive of plasma catecholamine levels, particularly NE, under a variety of stressful conditions, and may be a more direct and simple end point of catecholamine activity than are changes in heart rate.

Chromatography, High Pressure Liquid↗
PubMed1987

Synthesis and secretion of amylase in the rat parotid gland following autonomic nerve stimulation in vivo.

Parasympathetic and sympathetic nerve stimulation in vivo, individually and in combination, was used to study secretion and synthesis of amylase in the rat parotid gland. After 30 min with sympathetic nerve stimulation (3 Hz) a decrease in glandular amylase was seen, which corresponded approximately to the salivary output. On the other hand, after parasympathetic stimulation (10 Hz), chosen to obtain comparable amylase output, there was no decrease in glandular amylase, which points to synthesis during such activation. Experiments with incorporation of [3H]leucine, reflecting amylase synthesis, showed that both types of nerve stimulations increased such uptake in parotid protein. These results indicate that beside sympathetic activity, which is the main stimulus for granular amylase secretion, parasympathetic nerve impulses can evoke considerable amylase secretion because amylase synthesis is stimulated and amylase is rapidly available from a special, possibly non-granular pool. As expected from previous experiments an augmentation of amylase secretion was found, and the present experiments also indicated an augmentation at the level of synthesis when the two nerves were stimulated at the same time.

Amylases↗
PubMed1989

Parasympathetic activation of amylase secretion in the intact and sympathetically denervated rat parotid gland.

Observations were made on amylase secretion from the rat parotid gland induced by parasympathetic nerve stimulation in vivo. In spite of a low salivary amylase concentration a large total amylase output, equivalent to 36% of initial gland content, was found on prolonged activation (5 Hz, 120 min). However, no decrease in gland amylase content was found, which indicates that the output of amylase was balanced by synthesis. We suggest that prolonged, parasympathetically induced amylase secretion is dependent on activation of amylase synthesis and that the secretion is mainly of non-granular origin. Parasympathetic nerve stimulation produced an even larger amylase output from sympathectomized glands. Even under these conditions gland amylase content was unchanged and no obvious degranulation was found when the glands were examined after stimulation. This is in marked contrast to the decrease in amylase content and to the degranulation which are found after sympathetic activation.

Amylases↗
PubMed1980

Parotid secretion of fluid and amylase in rabbits during feeding.

Saliva has been collected from conscious rabbits in response to feeding pellets and carrots and amylase concentrations and flow-rates were measured. Saliva was collected from a polythene tube permanently inserted into the main duct, which, in most cases, kept patent for about a fortnight without any obvious decrease in the secretory capacity of the glands. 2. With pellets the flow-rate varied between 50 and 1250 microliter./min, and the corresponding amylase concentration was relatively constant around 250 units/ml. When carrots were fed, the flow-rates were about threefold lower, but the amylase concentration was raised to a mean value around 1000 units/ml. In spite of the differences in flow-rates, the two kinds of food promoted the same maximum output of amylase, and the output for both kinds of food promoted the same maximum output of amylase, and the output for both kinds of food was found to increase with the flow-rate. 3. The amylase concentration in the saliva decreased after pre- or post-ganglionic sympathetic denervation, reducing the output of amylase by about 50%. However, the amylase concentration was further lowered by beta-adrenoceptor block, which decreased the output by an additional 25%, suggesting that circulating catecholamines contributed to the secretion of amylase. 4. The fluid secretion in response to pellets and carrots was mainly dependent on parasympathetic activity, and for both kinds of food the range of flow-rates was unaltered by sympathectomy or beta-adrenoceptor block. However, at flow-rates below 50 microliter./min, where 25% of all samples with carrots were obtained, sympathetic activity may have contributed significantly to the fluid secretion. 5. In experiments on anaesthetized rabbits, frequency-response curves for amylase and fluid secretion in response to parasympathetic and sympathetic activation were obtained. A comparison between these observations and those obtained in the conscious animals during feeding suggests a parasympathetic activity mainly between 1 and 5 Hz and a sympathetic around 1 Hz. 6. It is concluded that both parasympathetic and sympathetic secretory nerves are reflexly activated during feeding, and that the normal secretion during a meal is dependent on an interplay between the nerves. The results suggest that at least two different afferent nervous pathways are involved in the control of the secretory nerves.

Amylases↗
PubMed1993

Regulation and cloning of the gene encoding amylase activity of the ruminal bacterium Streptococcus bovis.

Streptococcus bovis is an important starch-degrading ruminal bacterium that has been implicated as being important in the etiology of a number of ruminal pathologies associated with diets high in grains. Previous studies with S. bovis have shown that amylase production was influenced by the growth substrate, but the nature of this regulation was not determined. The current study was conducted to better describe the regulatory phenomena and gain a better understanding of the molecular characteristics of this activity. Nutritional experiments demonstrated that the presence of starch or the starch-derived disaccharide maltose was required for maximum amylase production. Subsequent time-course experiments showed that amylase synthesis was induced by maltose and repressed by glucose, cellobiose, and fructose, while inulin and lactose had little effect on enzyme accumulation. The effects of the added antibiotics rifampin and tetracycline were consistent with transcriptional control of amylase synthesis. Analysis of S. bovis cells grown on glucose or maltose showed that they contained similar low levels of cyclic AMP, indicating that it was unlikely that regulation of amylase synthesis was mediated through a mechanism involving this nucleotide. The amylase gene from S. bovis JB1 was cloned and expressed in Escherichia coli. The amylase produced in E. coli was of lower molecular weight than that synthesized by S. bovis and had catalytic characteristics different from those of S. bovis amylase. When the gene was introduced back into S. bovis JB1, only one form of amylase activity was detected, indicating that the entire gene was present on this insert. The use of the amylase gene as a genetic probe for identification of S. bovis strains is discussed.

Amylases↗