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PubMed1976

The mechanism of increased renal clearance of amylase in acute pancreatitis.

Amylase isoenzymes, separated by polyacrylamide gel electrophoresis, were measures in 25 normal persons (mean amylase to creatinine clearance ratio 3.0%), 15 patients with acute pancreatitis (mean clearance ratio 9.5%, P less than 0.0001), and 6 patients with hyperamylasemia due to common duct stones (mean clearance ratio 4.1%). Two isoamylases (P1, P2) resembling pancreatic isoenzymes and three isoamylases (S1, S2, S3) resembling salivary isoenzymes appeared regularly in normal serum and urine. Salivary amylases predominated in serum, but pancreatic amylases predominated in urine. This finding is consistent with renal clearance of pancreatic amylases exceeding that of salivary amylases under normal conditions. In patients with pancreatitis or common duct stones, essentially all of the increased amylase activity in serum and urine was due to pancreatic isoamylases (P1 and P2) in their normal proportions. No new or altered amylase isoenzymes were detected. The fraction of pancreatic amylases in the serum or urine was identical for the two diseases. Whereas the difference in amylase to creatinine clearance ratios observed between the two groups of patients is not a function of different amylase isoenzymes presented to the kidney, we conclude that the increased amylase clearance in acute pancreatitis is caused by an alteration of renal transfer of amylase, either at the glomerulus or tubule.

Acute Disease↗
PubMed1963

DE NOVO SYNTHESIS OF ALPHA-AMYLASE BY BACILLUS STEAROTHERMOPHILUS.

Welker, N. E. (Western Reserve University, Cleveland, Ohio and University of Illinois, Urbana), and L. Leon Campbell. De novo synthesis of alpha-amylase by Bacillus stearothermophilus. J. Bacteriol. 86:1202-1210. 1963.-The pH optimum for the synthesis of alpha-amylase by washed-cell suspensions was 6.7. alpha-Amylase synthesis began soon after the addition of the inducer (maltose, methyl-beta-d-maltoside, or phenyl-alpha-d-glucoside, at 10(-3)m), proceeded at a linear rate for 60 min, and then leveled off. Cell suspensions without inducer produced small amounts of alpha-amylase. The addition of glucose (2 x 10(-3)m), sucrose (10(-3)m), or glycerol (4 x 10(-3)m) to washed-cell suspensions failed to stimulate the production of alpha-amylase. Nitrogen starvation of washed cells for 60 min with fructose as a carbon source or by induction with pure maltose showed that the ability to produce alpha-amylase was lost. Examination of the amino acid pool at this time showed a general depletion of amino acids and the complete disappearance of tyrosine, phenyl-alanine, proline, and valine. Replenishment of the amino acid pool with casein hydrolysate (0.5%) restored the ability of the cells to produce alpha-amylase. Chloramphenicol and 8-azaguanine were shown to inhibit alpha-amylase synthesis. Inhibition was observed immediately upon the addition of chloramphenicol to cell suspensions preinduced for varying periods of time. Actinomycin D and mitomycin C also inhibited alpha-amylase synthesis when added to induced washed-cell suspensions. The amino acid analogues, norvaline, norleucine, and ethionine, inhibited alpha-amylase formation by 72, 53, and 38%, respectively. p-Fluorophenylalanine inhibited the synthesis of active alpha-amylase by 92% and the incorporation of proline-C(14) into alpha-amylase and cellular proteins by 95 and 74%, respectively.

Amino Acids↗
PubMed1989

beta-Amylase from Mustard (Sinapis alba L.) Cotyledons : Immunochemical Evidence for Synthesis de Novo during Photoregulated Seedling Development.

A polyclonal antiserum against mustard (Sinapis alba L.) beta-amylase was obtained by injecting a homogeneously purified enzyme preparation in rabbits. The formation of beta-amylase specific antibodies was confirmed by staining the precipitin line in double diffusion gel for beta-amylase activity. The monospecificity of antiserum against mustard beta-amylase was also ascertained by Western blotting. The antiserum efficiently recognised both the denatured and the native form of beta-amylase, but it did not cross-react with other higher plant beta-amylase. The mode of photoregulation of beta-amylase activity in mustard cotyledons was investigated by a variety of immunochemical techniques. Immunotitration experiments ruled out the possible contribution of enzyme activation/inactivation in photoregulation of beta-amylase activity. The use of single radial immunodiffusion, rocket immunoelectrophoresis, and immunotitration confirmed that the light mediated increase in beta-amylase activity quantitatively corresponds with the increase in beta-amylase protein level. The in vivo labeling with l-[(35)S] methionine and pulse chase studies of in vivo labeled beta-amylase protein revealed that the photoregulated increase in beta-amylase activity in mustard cotyledon exclusively results from an increase in the rate of de novo synthesis of beta-amylase protein against a very low background rate of enzyme degradation.

Journal Article↗
PubMed1990

Amylases in Pea Tissues with Reduced Chloroplast Density and/or Function.

Pea (Pisum sativum L.) tissues with reduced chloroplast density (e.g. petals and stems) or function (i.e. senescent leaves and leaves darkened for prolonged periods) were surveyed to determine whether tissues with genetically or environmentally reduced chloroplast density and/or function also have significantly different amylolytic enzyme activities and/or isoform patterns than leaf tissues with totally competent chloroplasts. Native PAGE followed by electrophoretically blotting through a starch or beta-limit dextrin containing gel and KI/I(2) staining revealed that the primary amylases in leaves, stems, petals, and roots were the primarily vacuolar beta-amylase (EC 3.2.1.2) and the primarily apoplastic alpha-amylase (EC 3.2.1.1). Among tissues of light grown pea plants, petals contained the highest levels of total amylolytic (primarily beta-amylase) activity and considerably higher ratios of beta- to alpha-amylase. In aerial tissues there was an inverse relationship between chlorophyll and starch concentration, and beta-amylase activity. In sections of petals and stems there was a pronounced inverse relationship between chlorophyll concentration and the activity of alpha-amylase. Senescing leaves of pea, as determined by age, and protein and chlorophyll content, contained 3.8-fold (fresh weight basis) and 32-fold (protein basis) higher alpha-amylase activity than fully mature leaves. Leaves maintained in darkness for 12 days displayed a 14-fold (fresh weight basis) increase in alpha-amylase activity over those grown under continuous light. In senescence and prolonged darkness studies, the alpha-amylase that was greatly increased in activity was the primarily apoplastic alpha-amylase. These studies indicate that there is a pronounced inverse relationship between chloroplast function and levels of apoplastic alpha-amylase activity and in some cases an inverse relationship between chloroplast density and/or function and vacuolar beta-amylase activity.

Journal Article↗
PubMed2002

Electrophoretically unique amylases in rat livers: phylogenic and ontogenic study on the mammalian liver.

Liver amylase activity in rodents was assayed with Blue Starch as substrate, and found to be higher than in humans or pigs. Based on the result of concanavalin A affinity chromatography, we found that the sugar moieties of amylase molecules increased in parallel with amylase activity in the tested mammals. However, the amounts of amylase proteins determined by Western bloting with anti-human salivary-type antibody as the probe, were similar to the levels in mammalian livers. Moreover, a similar expression of amylase mRNA was also detected in the mammalian livers by a reverse transcriptional-polymerase chain reaction using primers specific for the human salivary and/or pancreatic amylase complementary DNA (cDNA) sequences. The amylase was detected at the catalytic activity, protein molecule and mRNA levels in rat liver at all ages from fetus to adult. Salivary-type liver amylase activity increased up to one week after birth, and was maintained at the adult level thereafter. However, based on the results of the electrophoretic mobility test, livers with accelerated amylase activity, e.g., at 2-4 weeks after birth or during liver regeneration after partial hepatectomy, were also found to express an amylase electrophoretical identical to pancreatic-type amylase in addition to salivary-type activity. These results suggest that the liver may express an etopic amylase in a certain condition.

Amylases↗
PubMed1994

Rapid measurement of serum pancreatic amylase.

A simple, rapid assay for the pancreatic isoenzyme of human serum amylase was developed. The assay utilized an immunoabsorbent prepared by coating latex beads with a monoclonal antibody specific for pancreatic amylase. Treatment of patient serum with immunoabsorbent removed pancreatic amylase, and measurement of residual amylase activity with standard total amylase methodology allowed estimation of the pancreatic amylase content. Extraction efficiency of pancreatic amylase was consistent at amylase concentrations up to 1,000 U/L (y = 0.97 x +16.7 U/L; r = 0.9995). The assay was standardized with purified pancreatic amylase added to neonatal serum (low endogenous activity). A comparison of patient specimen results with the results of a standard technique (cellulose acetate electrophoresis) yielded an excellent correlation (immunoabsorption result = 0.96 electrophoresis result + 1.2 U/L; r = 0.987). Salivary amylase did not interfere with the assay until levels exceeded 1,000 U/L. Daily analysis of a frozen serum pool yielded a coefficient of variation of 9.2% at mean pancreatic amylase value of 54 U/L (+/- 5 U/L). A normal range study found a strong influence of age, with pancreatic amylase levels increasing dramatically in the first 3 years of life, to stabilize at a range of 0-66 U/L thereafter.

Amylases↗
PubMed1984

Metabolism of glycosylated human salivary amylase: in vivo plasma clearance by rat hepatic endothelial cells and in vitro receptor mediated pinocytosis by rat macrophages.

Salivary-type amylase normally comprises about 60% of the amylase activity in human serum, but only a small fraction is a glycosylated isoenzyme (amylase A). In contrast, 1/3 of amylase in human saliva is glycosylated. Since glycosylation can affect circulatory clearance, we studied the clearance of amylase A in rats and its uptake by rat alveolar macrophages. Following intravenous injection, 125I-labeled amylase A disappeared rapidly from plasma (t 1/2 = 9 min) and accumulated in the liver. Simultaneous injection of mannose-albumin slowed its clearance to a rate comparable to that of 125I-labeled nonglycosylated salivary amylase (t 1/2 = 45 min). In contrast, galactose-albumin had no effect. Electron microscope autoradiography of the liver following injection of 125I-labeled amylase A revealed a localization of grains over the hepatic endothelial cells. In vitro studies indicated that amylase A is taken up by alveolar macrophages via receptor-mediated pinocytosis. Uptake was linear over time, saturable, and inhibited by mannan and mannose-albumin, but not by galactose-albumin. We conclude that amylase A, which is a naturally occurring human glycoprotein with at most three terminal L-fucose residues per molecule, is recognized in rats by a mannose receptor located on hepatic endothelial cells. We speculate that this receptor, by rapidly clearing circulating amylase A, may be responsible for the low level of amylase A in human serum.

Amylases↗
PubMed1976

Properties of the amylase produced in carcinoma of the lung.

The properties of the amylase produced by carcinoma of the lung were studied. The abnormal amylase recognized in the serum of a patient with carcinoma of the lung had a mobility with beta-position and showed reduced migration to the cathodic side after neuraminidase digestion. This abnormal amylase had a close affinity for Concanavalin A and this affinity was not retarded by the neuraminidase digestion. However, the purified, tumor-extracted, amylase from the same patient had the same electrophoretic migration as normal human salivary amylase and was not affected by neuraminidase treatment. The abnormal affinity for Concanavalin A was not observed in this purified tumor-extracted amylase. It is suggested that some transglycosidation steps are needed for the appearance of the abnormal amylase in the patient's serum, and that the terminal sialic acid is independent of the affinity for Concanavalin A. The dissociation constants of the tumor amylase for several substrates were smaller than those of normal pancreatic or salivary amylases. Moreover, maltotriose had no affinity for the tumor-extracted amylase and it was not digested to maltose and glucose by the purified tumor extracted amylase. These differences in the kinetic properties and in the mode of digestion were of interest in the study of tumor-produced amylases.

Adenocarcinoma↗
PubMed2005

Serum amylase, pancreatic stents, and pancreatitis after sphincter of Oddi manometry.

BACKGROUND: Serum amylase levels 2 hours after ERCP predict postprocedure pancreatitis. The value of serum amylase measurements after sphincter of Oddi manometry (SOM) and the effect of pancreatic-duct stent placement on serum amylase are unknown. METHODS: Records were reviewed for 88 SOM patients who had serum amylase measured 2 hours after the procedure. Post-SOM pancreatitis was defined as pain with a >3-fold elevation of serum amylase on the morning after SOM. "Possible pancreatitis" was defined as pain with a <3-fold elevation of serum amylase on the morning after SOM. RESULTS: Post-SOM pancreatitis and possible pancreatitis each occurred in 13% of the study cohort. Post-SOM pancreatitis was associated with the absence of a pancreatic stent and occurred in 0% of patients without a stent who had normal 2-hour serum amylase vs. 67% with elevated 2-hour serum amylase (p < 0.01). Among patients who received a stent, pancreatitis occurred in 6%, regardless of whether the 2-hour serum amylase was elevated. Possible pancreatitis occurred mainly in patients who received stents, and it also was associated with elevation of the 2-hour serum amylase. CONCLUSIONS: Elevation of the serum amylase level 2 hours after SOM predicts post-SOM pancreatitis but only in patients who do not receive a pancreatic stent. Among patients who received a stent, elevated 2-hour serum amylase levels predict subsequent findings that may be caused by attenuated pancreatitis.

Adolescent↗
PubMed1984

Effects of some alpha-adrenoceptor stimulating and blocking agents on the salivary amylase secretion in the rabbit.

In rabbits under urethane anaesthesia parotid secretion of fluid and amylase in response to electrical stimulation of the sympathetic and parasympathetic nerves was measured before and after injections of various agents acting on alpha-adrenoceptors. Amylase secretion in response to sympathetic nerve stimulation at 0.5 and 1 Hz was markedly reduced by clonidine, 0.5-30 micrograms/kg, in a dose related manner. The effect was not due to an altered responsiveness of the gland, since isoprenaline still caused a large release of amylase. Phenylephrine, 10 micrograms/kg, and prazosine, 300 micrograms/kg, had no effect on the sympathetically evoked amylase secretion. Yohimbine in a dose of 0.5 mg/kg increased the amylase output in response to sympathetic nerve stimulation at 0.5 Hz by 70%, while the response at 1 Hz, which is close to maximum for the gland, was not significantly increased. The fluid and amylase secretion produced by parasympathetic nerve stimulation at 1.5, 5.0 and 10 Hz remained unchanged after clonidine, 1.0-30 micrograms/kg, or yohimbine 0.5 mg/kg. In rabbits provided with chronic parotid fistulae fluid and amylase secretion were studied after injections of clonidine, 30 micrograms/kg, and yohimbine, 1 mg/kg. In the conscious animal clonidine reduced not only amylase but also fluid secretion, by around 50 and 30%, respectively, indicating an effect on the activity in both the sympathetic and parasympathetic secretory nerves. Yohimbine increased the output of amylase during feeding, seen as an increased mean output of amylase due to an increased concentration of amylase in the saliva, while fluid secretion remained unchanged. The various experiments suggest that amylase secretion in response to sympathetic activation may be influenced by prejunctional control of transmitter release via alpha-2-adrenoceptors, and that this control may be of physiological significance. Parasympathetically evoked secretion does not seem to be under the influence of a similar control.

Adrenergic alpha-Agonists↗
PubMed1989

Genetic analysis of the promoter region of the Bacillus subtilis alpha-amylase gene.

The amyR2 allele of the Bacillus subtilis alpha-amylase cis-regulatory region enhances production of amylase and transcription of amyE, the structural gene, by two- to threefold over amyR1. The amylase gene bearing each of these alleles was cloned on plasmids of about 10 to 15 copies per chromosome. Transcription of the cloned amylase gene by each amyR allele was activated at the end of exponential growth and was subject to catabolite repression by glucose. The amount of amylase produced was roughly proportional to the copy number of the plasmid, and cells containing the amyR2-bearing plasmid, pAR2, produced two- to threefold more amylase than cells with the amyR1 plasmid, pAMY10. Deletion of DNA 5' to the alpha-amylase promoter, including deletion of the A + T-rich inverted repeat found in amyR1 and amyR2, had no effect on expression or transcription of alpha-amylase. Deletion of DNA 3' to the amyR1 promoter did not impair temporal activation of chloramphenicol acetyltransferase in amyR1-cat-86 transcriptional fusions, but catabolite repression was abolished. When an 8-base-pair linker was inserted in pAMY10 at the same site from which the 3' deletion was made, amylase expression doubled and was repressed less by glucose. Both the deletion and the insertion disrupted four bases at the 3' end of the putative amylase operator region. Site-directed mutagenesis was used to change bases in the promoter-operator region of amyR1 to their amyR2 counterparts. Either change alone increased amylase production twofold, but only the change at +7, next to the linker insertion of 3' deletion site, yielded the increased amylase activity in the presence of glucose that is characteristic of the amyR2 strain. The double mutant behaved most like strains carrying the amyR2 allele.

Bacillus subtilis↗
PubMed1988

Renal disposition of amylase, lipase, and lysozyme in the dog.

Normal adult dogs were given intravenously lysine hydrochloride to abolish renal tubular reabsorption. The treatment caused tubular proteinuria. Once forced diuresis was established, fractional clearances for amylase, lipase, and lysozyme increased five-, 18-, and 857-fold over the baseline values, respectively. There was relatively little tubular reabsorption of amylase, and urinary amylase activity remained low. A renal arteriovenous difference in amylase activity was not present. Urinary amylase activity could not be reactivated by the addition of serum or treatment with dithiothreitol. Urinary inhibitors of amylase activity were not detected. Immunoreactive urinary amylase did not exceed kinetically measured urinary amylase. Therefore, the presence of irreversibly inactivated amylase did not explain the low fractional clearance of amylase. A small amount of serum macroamylase was present, but macroamylasemia did not account for canine amylase failing to pass the glomerular filter. It appears that the renal loss of amylase in the dog is not an important excretory route.

Amylases↗
PubMed1984

Mechanism of regulation of amylase release by alpha- and beta-adrenergic agonists in rat parotid tissue.

The effect of forskolin and isobutyl-methylxanthine on amylase release and cyclic AMP accumulation by alpha- and beta-adrenergic agonists was studied in rat parotid slices. A small increase in cyclic AMP by beta-adrenergic agonists was sufficient for maximum stimulation of amylase release (Yoshimura et al., 1982a), but a similar increase in cyclic AMP by forskolin did not stimulate the maximum amount of amylase release. The amount of amylase release and cyclic AMP changed in parallel when lower doses of isobutyl-methylxanthine were used, but higher doses of isobutyl-methylxanthine further increased cyclic AMP without causing a significant increase in amylase release. Amylase release stimulated to its maximum by isobutyl-methylxanthine was much lower than that by isoproterenol. These results suggest that cyclic AMP is not the only chemical correlate for the activation of amylase release by beta-adrenergic agonists. The effect of phenylephrine and methoxamine on amylase release was augmented by either forskolin or isobutyl-methylxanthine, but the effect of methacholine was not. Phenylephrine increased the cyclic AMP concentration under the same conditions, but methoxamine did not. The inhibition of the effect of phenylephrine plus forskolin on cyclic AMP accumulation by propranolol was almost complete and stereospecific, but the inhibition of their effects on amylase release was incomplete and not stereospecific. Synergism of amylase release was observed in the effect between methoxamine and dibutyryl-cyclic AMP. These results suggest that the augmentation of the effect of alpha-adrenergic agonists on amylase release by forskolin or isobutyl-methylxanthine cannot be explained only on changes in cyclic AMP and that some other factor in collaboration with cyclic AMP may participate in the regulation of amylase release by alpha-adrenergic agonists.

1-Methyl-3-isobutylxanthine↗
PubMed1995

Endogenous amylase levels and response to supplemental feed enzymes in male turkeys from hatch to eight weeks of age.

Amylase and xylanase enzyme concentrations in the pancreas, small intestine, and crop were measured in Nicholas male poults fed diets with and without supplemental amylase and xylanase from 0 to 8 wk of age. Eight birds from each of three diets (control, amylase-supplemented, xylanase-supplemented) were killed every 3 d to determine the amylase and xylanase activity within the pancreas, small intestine, and crop. Pancreatic organ weight was not affected by diet, indicating an absence of dietary amylase effect upon pancreatic tissue growth. Pancreatic amylase activity was not consistently affected by diet. Amylase activity within the intestinal chyme increased sporadically with dietary amylase supplementation over the control and xylanase-supplemented diets. Increasing supplemental amylase activity levels may provide more conclusive evidence of an additive effect of dietary amylase and endogenous amylase activity. Xylanase supplementation within the feed did not affect endogenous amylase activity.

Amylases↗
PubMed2001

Purification and characterization of alpha-amylases from the intestine and muscle of ascaris suum (Nematoda).

Alpha-Amylase (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of pigs Ascaris suum. The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of a-amylase from muscles with pl of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. SDS/PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of a-amylases from intestine and 59 kDa for the muscle enzyme. Alpha-Amylase from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal alpha-amylase. Both the muscle and intestine amylase lost half of its activity after 15 min at 70 degrees C and 50 degrees C, respectively. The Km values were: for muscle amylase 0.22 microg/ml glycogen and 3.33 microg/ml starch, and for intestine amylase 1.77 microg/ml glycogen and 0.48 microg/ml starch. Both amylases were activated by Ca2+ and inhibited by EDTA, iodoacetic acid, p-chloromercuribenzoate and the inhibitor of a-amylase from wheat. No significant differences were found between the properties of a-amylases from parasites and from their hosts.

Animals↗
PubMed2002

Kinetic analysis of icodextrin interference with serum amylase assays.

Patients treated with Extraneal peritoneal dialysis solution (Baxter Healthcare Corporation, Deerfield, IL, U.S.A.) have a significant decrease in serum amylase activity. The decline is reported to be due to interference of icodextrin in a routinely used laboratory assay. The present study was designed to investigate the kinetics of icodextrin interference in the amylase activity assay and to determine whether assay interference can account for the total decline in amylase activity. Plasma obtained from healthy volunteers was spiked with 0, 0.21, 0.71, and 3.6 mg/mL icodextrin. Amylase activity was determined using Sigma kit 577-10 (Sigma Diagnostics, St. Louis, MO, U.S.A.). Amylase activity in plasma samples spiked with 3.6 mg/mL icodextrin was also monitored while varying the concentration of the substrate (ET-G7-PNP) from the assay kit. Amylase activity decreased with increasing amounts of icodextrin and decreasing amounts of assay substrate. A 72.6% decrease in amylase activity was observed in samples spiked with 3.6 mg/mL icodextrin as compared with samples without icodextrin at a substrate level similar to that in the assay kit (0.71 mmol/L). Double reciprocal and Dixon plots indicate competitive inhibition of amylase activity by icodextrin. Icodextrin functions as a competitive inhibitor in the assay for amylase activity, as predicted by the structural similarities between icodextrin and the amylase assay substrate. The degree of icodextrin interference suggests that the entire decline in amylase activity observed in patients using Extraneal can be accounted for qualitatively by icodextrin interference. The amylase activity decline in patients treated with Extraneal is an artifact attributable to assay interference.

Amylases↗
PubMed1987

Impairment of starch absorption by a potent amylase inhibitor.

Many previous investigations of available amylase inhibitors have not been able to demonstrate significant carbohydrate malabsorption. This study uses breath hydrogen analysis, a sensitive method for detecting the passage of starch into the colon, to determine if a potent amylase inhibitor is capable of producing carbohydrate malabsorption. Thirteen volunteers underwent three studies, ingesting as a carbohydrate substrate: lactulose 20 g, spaghetti alone, and spaghetti with amylase inhibitor (3.8 g). Samples of breath were collected (at frequent intervals) for 2 h after the lactulose and for 8 h after the spaghetti meal and analyzed for hydrogen concentration. The ingestion of spaghetti alone resulted in significant increases in breath hydrogen concentration at 420-450 min. The mean (+/- SE) hydrogen excretion rate was increased more than 2-fold with the amylase inhibitor, from 0.4 +/- 0.2 to 0.9 +/- 0.3 ml/h (p less than 0.05). Use of the amylase inhibitor in powder form produced a similar increase in the rate of hydrogen excretion to 1.1 +/- 0.4 ml/h. The percentage of carbohydrate malabsorbed was calculated for the spaghetti meal and spaghetti with amylase inhibitor using each individual's observed hydrogen excretion with lactulose. Over the 8-h observation period, 4.7 +/- 1.9% of the spaghetti was malabsorbed and 7.0 +/- 1.4% of the spaghetti with amylase inhibitor was malabsorbed (p less than 0.05). Measurements of the effect of the amylase inhibitor on amylase activity of duodenal juice revealed that the amylase inhibitor at a concentration of more than 5 mg/ml decreased the amylase activity by more than 96%. These results indicate that this potent amylase inhibitor is capable of enhancing malabsorption of wheat starch.

Adult↗
PubMed1985

Rapid quantitative, specific measurement of pancreatic amylase in serum with use of a monoclonal antibody.

In this rapid quantitative assay for pancreatic alpha-amylase (EC 3.2.1.1) in serum, we precipitate salivary amylases by 10-min incubation with monoclonal anti-salivary amylase antibody immobilized on particles of polyvinylidene fluoride. We then centrifuge the serum mixture and measure the pancreatic amylase activity remaining in the supernate by a kinetic method. The assay requires 50 microL of serum and the standard curve is linear to at least 1300 U of pancreatic amylase per liter of serum. CVs were 1.3% within-run, 6-8% day-to-day. Apparent analytical recovery of pancreatic amylase activity added to serum was 101% +/- 2%. Addition of purified salivary amylase, 356 U/L, to sera gave a value for apparent pancreatic amylase of less than 4 U/L, or 1% of the added salivary amylase activity. This assay correlated well with an electrophoretic method (slope, 0.97-0.99; intercept, 0.5 to -4 U/L; correlation coefficient, 0.946-0.990; and standard error of the estimate 3-5 U/L). Estimated normal reference intervals with maltotetraose as substrate were: total amylase, 39-118 U/L; pancreatic amylase, 11-50 U/L; and salivary amylase, 18-79 U/L.

Antibodies, Monoclonal↗