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PubMed1992

Antigen specificity and cross-reactivity of fifteen monoclonal antibodies against porcine pancreatic alpha-amylase II and its AB and C domains.

Highly productive hybridoma secreting mabs specific for porcine alpha-pancreatic amylase II were established. Fifteen clones were selected. The mabs produced (KD = 1.68-11.2 nM) were checked for cross-reactivity with six heterologous antigens, namely porcine pancreatic alpha-amylase I, barley amylase, human pancreatic alpha-amylase, Taka amylase and triose phosphate isomerase, using direct ELISA assay; mabs were classified within seven groups: in a few groups mabs cross-reacted with a single heterologous antigen either porcine pancreatic amylase I (6 mabs) or barley amylase (2 mabs) or human pancreatic amylase (3 mabs). Two other groups cross-reacted with two heterologous antigen either porcine I and human or porcine I and barley. Only one mab out of fifteen cross-reacted in direct ELISA binding to all amylases and triose phosphate isomerase. Using sandwich ELISA test only three mabs were found to bind porcine amylase II present at high concentration. Results consistent with direct porcine amylase binding were obtained from binding inhibition assays. Analysis by the additivity test allowed to find that 3 mabs, B10.10, B1.11, C6.4 recognize distinct epitopes while the epitopes for the other pairs tested are either overlapping or at least close to each other. Finally mabs binding specifically either to the AB or to the C domain fragment or to both fragments have been obtained.

Animals↗
PubMed1979

Genetic variation in amount of salivary amylase in the bank vole, Clethrionomys glareola.

Several investigated bank vole populations are polymorphis for the number of salivary amylase loci, and individual chromosomes may carry one, two or three linked amylase structural genes. In the present study, we have used bank vole stocks homozygous for different chromosomes to investigate the relationship between amylase production and gene number. By measuring the amylase activity in parotid glands and the percentage of amylase protein in saliva, we have been able to demonstrate that the amount of salivary amylase is directly proportional to the proposed gene number. The paper also describes the allele, AmySu, which codes for a heat-labile salivary amylase. The relative amounts of the heat-labile isozyme have been determined in different heterozygotes containing this allele, and these results also support the multiple locus model. Finally, a stock devoid of salivary amylase activity was established. Animals from this strain have, however, a protein in the parotid glands and in saliva that is very similar to amylase in molecular weight, amino acid composition and in its binding to glycogen and cyclohepta-amylose. In genetic crosses, the protein segregates as an amylase allele. Therefore, this protein, encoded by the functionally null allele AmyN, may represent an incorrectly processed amylase precursor.

Amylases↗
PubMed1995

Role of the C-terminal region of beta-amylase from barley.

To investigate the role of the C-terminal region of barley beta-amylase, plasmid delta 54 was constructed with an expression vector (pBETA92) of barley beta-amylase by site-directed mutagenesis. Escherichia coli JM109 harboring plasmid delta 54 was expected to express delta 54 beta-amylase in which 54 amino acid residues were deleted from the C-terminus. The enzyme production started in the logarithmic phase, increased linearly, and reached a maximum after 12 h. delta 54 beta-amylase gave a single activity band on isoelectric focusing (pI 6.85). delta 54 beta-amylase was purified from the cells by consecutive alpha-cyclodextrin/Sepharose 6B column chromatography. A comparison of the properties of the mutant enzyme with those of the original recombinant beta-amylase [Biosci. Biotech. Biochem. (1994) 58, 1080-1086] revealed two major differences. First, the original recombinant beta-amylase showed heterogeneity on isoelectric focusing, but delta 54 beta-amylase gave a single main band of protein (pI 6.85). Therefore, the isoelectrophoretic heterogeneity of the original recombinant beta-amylase was apparently due to its C-terminal region. Secondly, delta 54 beta-amylase lacked thermostability. Therefore, it was concluded that the C-terminal region was significantly involved in the thermostability of beta-amylase.

Base Sequence↗
PubMed1994

alpha-Amylases from Thermoactinomyces vulgaris: characteristics, primary structure and structure prediction.

Two amylolytic active protein fractions (named alpha-amylase 1 and alpha-amylase 2) were isolated from the bacterium Thermoactinomyces vulgaris strain 94-2A. alpha-Amylase 1 had a molecular mass of 51.6 kDa, whereas alpha-amylase 2 consists of two fragments which have molecular masses of 17.0 and 34.6 kDa, respectively. These two fragments are products from a proteolytic cleavage of alpha-amylase 1 at amino acid position 303 (tryptophan) by a serine protease (thermitase) which is also produced by T. vulgaris. The purified alpha-amylase 1 and 2 follow the Michaelis-Menten kinetics in the presence of starch as substrate with Km values of 1.37 +/- 0.07 and 1.29 +/- 0.18 mg/mL, respectively. In effect they differ in their stability characteristics. The amino acid sequence of alpha-amylase from T. vulgaris derived from DNA sequence (1) was compared with those of other alpha-amylases. It reveals high homologies to alpha-amylases from other microorganisms (e.g. B. polymyxa, A. oryzae, S. occidentalis and S. fibuligera). A three-dimensional structure model for alpha-amylase 1 on the basis of the 3 A X-ray structure of Taka-amylase was constructed.

Amino Acid Sequence↗
PubMed1989

The diagnostic significance of increased urinary and serum amylase activity in bitches with pyometra.

The serum amylase and the serum lipase activities determined simultaneously were normal in 92 bitches with pyometra (group A). To determine the usefulness of the information provided by the measurement of urinary amylase activity in pyometra dogs, the relation of serum and urinary amylase activity to urinary protein and serum lipase activity in paired serum and urine samples was investigated in 39 control bitches and in a second group of 66 bitches with pyometra (group B). The 39 control bitches and 18 pyometra bitches (group B1) had normal urinary amylase activity and showed neither a change in urinary protein nor in serum amylase or lipase activities. There was no relationship between the urinary amylase activity and the urinary protein level or the serum amylase activity. The remaining forty-eight pyometra bitches (group B2) had normal serum lipase activity and increased urinary amylase activity (amylasuria), which correlated highly with the increased urinary protein concentration and to a lesser degree with the increased serum amylase activity. Renal failure in 15 of those bitches had no influence on the degree of increase in the urinary or serum amylase activity. It was concluded that, in the absence of any significant indication of pancreatic disease, amylasuria and amylasaemia in bitches with pyometra are a strong indication of renal glomerular disease. Amylasuria was indicative to some degree of an increased serum amylase activity, but was unrelated to renal failure.

Amylases↗
PubMed1991

Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c.

A Butyrivibrio fibrisolvens amylase gene was cloned and expressed by using its own promoter on the recombinant plasmid pBAMY100 in Escherichia coli. The amylase gene consisted of an open reading frame of 2,931 bp encoding a protein of 976 amino acids with a calculated Mr of 106,964. In E. coli(pBAMY100), more than 86% of the active amylase was located in the periplasm, and TnphoA fusion experiments showed that the enzyme had a functional signal peptide. The B. fibrisolvens amylase is a calcium metalloenzyme, and three conserved putative calcium-binding residues were identified. The amylase showed high sequence homology with other alpha-amylases in the three highly conserved regions which constitute the active centers. These and other conserved regions were located in the N-terminal half, and no similarity with any other amylase was detected in the remainder of the protein. Deletion of approximately 40% of the C-terminal portion of the amylase did not result in loss of amylolytic activity. The B. fibrisolvens amylase was identified as an endo-alpha-amylase by hydrolysis of the Phadebas amylase substrate, hydrolysis of gamma-cyclodextrin to maltotriose, maltose, and glucose and the characteristic shape of the blue value and reducing sugar curves. Maltotriose was the major initial hydrolysis product from starch, although extended incubation resulted in its hydrolysis to maltose and glucose.

Amino Acid Sequence↗
PubMed1995

The S-layer from Bacillus stearothermophilus DSM 2358 functions as an adhesion site for a high-molecular-weight amylase.

The S-layer lattice from Bacillus stearothermophilus DSM 2358 completely covers the cell surface and exhibits oblique symmetry. During growth of B. stearothermophilus DSM 2358 on starch medium, three amylases with molecular weights of 58,000, 98,000, and 184,000 were secreted into the culture fluid, but only the high-molecular-weight enzyme was found to be cell associated. Studies of interactions between cell wall components and amylases revealed no affinity of the high-molecular-weight amylase to isolated peptidoglycan. On the other hand, this enzyme was always found to be associated with S-layer self-assembly products or S-layer fragments released during preparation of spheroplasts by treatment of whole cells with lysozyme. The molar ratio of S-layer subunits to the bound amylase was approximately 8:1, which corresponded to one enzyme molecule per four morphological subunits. Immunoblotting experiments with polyclonal antisera against the high-molecular-weight amylase revealed a strong immunological signal in response to the enzyme but no cross-reaction with the S-layer protein or the smaller amylases. Immunogold labeling of whole cells with anti-amylase antiserum showed that the high-molecular-weight amylase is located on the outer face of the S-layer lattice. Because extraction of the amylase was possible without disintegration of the S-layer lattice into its constituent subunits, it can be excluded that the enzyme is incorporated into the crystal lattice and participates in the self-assembly process. Affinity experiments strongly suggest the presence of a specific recognition mechanism between the amylase molecules and S-layer protein domains either exposed on the outermost surface or inside the pores. In summary, results obtained in this study confirmed that the S-layer protein from B. stearothermophilus DSM 2358 functions as an adhesion site for a high-molecular-weight amylase.

Amylases↗
PubMed1991

Clinical and immunological responses to occupational exposure to alpha-amylase in the baking industry.

alpha-Amylase is a starch cleaving enzyme often used in the baking industry as a flour additive. It is usually of fungal origin, produced by Aspergillus oryzae. One previous report has shown IgE antibodies and positive skin prick test against alpha-amylase in asthmatic bakers. This paper describes four alpha-amylase sensitised index cases with occupational asthma or rhinitis and the results of a cross sectional study of 20 workers from the same factory who were also exposed to alpha-amylase powder. Air sampling detected airborne alpha-amylase at a concentration of 0.03 mg/m3. Significantly more work related symptoms such as rhinitis and dermatitis were found among the alpha-amylase exposed workers compared with referents. A skin prick test to alpha-amylase was positive in 30% (6/20) of the exposed workers. Most of the persons showing a positive skin prick test had work related symptoms and were also skin prick test positive to common allergens. Nasal challenge tests with amylase were performed in selected cases and validated three cases of alpha-amylase induced rhinitis. Two non-symptomatic workers had precipitins to alpha-amylase. Specific IgG antibodies were shown by two further serological techniques. The nature and relevance of these antibodies are currently being studied. It is concluded that alpha-amylase powder is a potent occupational sensitiser. Precautions should be taken when handling this allergenic enzyme.

Adult↗
PubMedDate not supplied

Relationship between adenosine 3',5'-cyclic monophosphate level, cell proliferation, and alpha-amylase in rat parotid.

Treatment of rats with isoproterenol (IPR, beta 1- and beta 2-agonist), dobutamine (beta 1-agonist), and terbutaline (beta 2-agonist) increased the cAMP level and cell proliferation, but it decreased alpha-amylase activity in parotid glands. Terbutaline was relatively less effective. Alpha-Amylase activity as determined by substrate hydrolysis was maximally depressed (85% of control) after 15 min of IPR treatment; however, alpha-amylase level as determined by Western immunoblotting with the primary antibody to alpha-amylase decreased maximally after 2 h of treatment. The level of alpha-amylase significantly decreased after 15 min of treatment, but the levels of alpha-amylase mRNAs of 702 and 1176 base pairs (bp) slightly increased at this time. This suggests that an increased rate of transcription or a decreased rate of degradation of alpha-amylase mRNAs without a proportional increase in the rate of translation of alpha-amylase occurs in parotid glands after treatment with IPR. The levels of alpha-amylase mRNAs decreased after 2 h of treatment; however, the level of alpha-mRNA of 702 bp continued to decline, but the level of alpha-mRNA of 1176 bp increased at 3 days after IPR treatment. The level of actin mRNA of 2200 bp increased at 15 min and remained elevated during the entire observation period. Results showed that IPR-induced elevation of cAMP increases cell proliferation, and alters the level and activity of alpha-amylase and the expression of alpha-amylase genes at different rates.

Actins↗
PubMed2004

Regulation of CCK-induced amylase release by PKC-delta in rat pancreatic acinar cells.

PKC is known to be activated by pancreatic secretagogues such as CCK and carbachol and to participate along with calcium in amylase release. Four PKC isoforms, alpha, delta, epsilon, and zeta, have been identified in acinar cells, but which isoforms participate in amylase release are unknown. To identify the responsible isoforms, we used translocation assays, chemical inhibitors, and overexpression of individual isoforms and their dominant-negative variants by means of adenoviral vectors. CCK stimulation caused translocation of PKC-alpha, -delta, and -epsilon, but not -zeta from soluble to membrane fraction. CCK-induced amylase release was inhibited approximately 30% by GF109203X, a broad spectrum PKC inhibitor, and by rottlerin, a PKC-delta inhibitor, but not by Gö6976, a PKC-alpha inhibitor, at concentrations from 1 to 5 microM. Neither overexpression of wild-type or dominant-negative PKC-alpha affected CCK-induced amylase release. Overexpression of PKC-delta and -epsilon enhanced amylase release, whereas only dominant-negative PKC-delta inhibited amylase release by 25%. PKC-delta overexpression increased amylase release at all concentrations of CCK, but dominant-negative PKC-delta only inhibited the maximal concentration; both similarly affected carbachol and JMV-180-induced amylase release. Overexpression of both PKC-delta and its dominant-negative variant affected the late but not the early phase of amylase release. GF109203X totally blocked the enhancement of amylase release by PKC-delta but had no further effect in the presence of dominant-negative PKC-delta. These results indicate that PKC-delta is the PKC isoform involved with amylase secretion.

Acetophenones↗
PubMed1983

Amylase in the saliva and in the gastric aspirates of premature infants: its potential role in glucose polymer hydrolysis.

Amylase activity was found in saliva from 13 infants, 26-42 wk corrected gestational age. The levels of salivary amylase activity increased with advancing age. In 10 infants, 31-38 wk corrected gestational age (estimated gestational age in wk plus age in wk after birth), gastric aspirates collected before a feeding and sequentially at 30-min intervals after two consecutive feedings were analyzed for amylase activity and pH. Two different postprandial patterns were obtained. For six of the 10 infants, both the pH and amylase activities of their gastric aspirates showed a distinct maxima at about 60 min after a feeding and a minima at 180 min just before the second feeding. In the remaining four infants, the pHs of their gastric aspirates remained relatively high (5.0-6.0) for the entire postprandial period. In these infants, there was a persistently high level of the amylase activity. In all 10 infants, amylase activity was found in their gastric aspirate samples when the pH was above 3.0. Comparison of the amylase in the gastric aspirate with purified pancreatic and salivary amylases by polyacrylamide gel electrophoresis showed that the amylase in the gastric aspirate has an electrophoretic mobility similar to that of salivary amylase, which suggests a salivary origin. This study supports the possibility that salivary amylase could enter the stomach and retain a significant amount of its activity in premature infants.

Amylases↗
PubMed2006

Effects of a dietary Aspergillus oryzae extract containing alpha-amylase activity on performance and carcass characteristics of finishing beef cattle.

Three experiments were conducted to examine the effects of an Aspergillus oryzae extract containing alpha-amylase activity on performance and carcass characteristics of finishing beef cattle. In Exp. 1, 120 crossbred steers were used in a randomized complete block design to evaluate the effects of roughage source (alfalfa hay vs. cottonseed hulls) and supplemental alpha-amylase at 950 dextrinizing units (DU)/kg of DM. Significant roughage source x alpha-amylase interactions (P < 0.05) were observed for performance. In steers fed cottonseed hulls, supplemental alpha-amylase increased ADG through d 28 and 112 and tended (P < 0.15) to increase ADG in all other periods. The increases in ADG were related to increased DMI and efficiency of gain during the initial 28-d period but were primarily related to increased DMI as the feeding period progressed. Supplemental alpha-amylase increased (P = 0.02) the LM area across both roughage sources. In Exp. 2, 96 crossbred heifers were used in a randomized complete block design with a 2 x 3 factorial arrangement of treatments to evaluate the effects of corn processing (dry cracked vs. high moisture) and supplemental alpha-amylase concentration (0, 580, or 1,160 DU/kg of DM). Alpha-amylase supplementation increased DMI (P = 0.05) and ADG (P = 0.03) during the initial 28 d on feed and carcass-adjusted ADG (P = 0.04) across corn processing methods. Longissimus muscle area was greatest (quadratic effect, P = 0.04), and yield grade was least (quadratic effect, P = 0.02) in heifers fed 580 DU of alpha-amylase/kg of DM across corn processing methods. In Exp. 3, 56 crossbred steers were used in a randomized complete block design to evaluate the effects of supplemental alpha-amylase (930 DU/kg of DM) on performance when DMI was restricted to yield a programmed ADG. Alpha-amylase supplementation did not affect performance when DMI was restricted. We conclude that dietary alpha-amylase supplementation of finishing beef diets may result in increased ADG through increased DMI under certain dietary conditions and that further research is warranted to explain its mode of action and interactions with dietary ingredients.

Animal Feed↗
PubMed1990

Where does serum amylase come from and where does it go?

The serum amylase concentration reflects the balance between the rates of amylase entry into and removal from the blood. Hyperamylasemia can result either from an increased rate of entry of amylase into the circulation and/or a decreased metabolic clearance of this enzyme. The pancreas and salivary glands have amylase concentrations that are several orders of magnitude greater than that of any other normal tissue, and these two organs probably account for almost all of the serum amylase activity in normal persons. A variety of techniques are now available to distinguish pancreatic from salivary-type isoamylase. Pancreatic hyperamylasemia results from an insult to the pancreas, ranging from trivial (cannulation of the pancreatic duct) to severe (pancreatitis). In addition, loss of bowel integrity (infarction or perforation) causes pancreatic hyperamylasemia due to absorption of amylase from the intestinal lumen. Hyperamylasemia due to salivary-type isoamylase is observed in conditions involving the salivary glands. In addition, this type of hyperamylasemia occurs in conditions in which there is no clinical evidence of salivary gland disease, such as chronic alcoholism, postoperative states (particularly postcoronary bypass), lactic acidosis, anorexia nervosa or bulimia, and malignant neoplasms that secrete amylase. Hyperamylasemia can also result from decreased metabolic clearance of amylase due to renal failure or macroamylasemia (a condition in which an abnormally high-molecular-weight amylase is present in the serum). Patients with abdominal pain and a markedly elevated serum amylase (more than three times the upper limit of normal) usually have acute pancreatitis, and additional serum enzyme testing is not helpful. Patients with smaller elevations of serum amylase often have conditions other than pancreatitis, and measurement of a serum enzyme more specific for the pancreas (pancreatitic isoamylase, lipase or trypsin) is frequently of diagnostic value in such patients.

Amylases↗
PubMed1988

Macroamylasemia with a markedly increased amylase clearance ratio in a patient with renal cell carcinoma.

We report hyperamylasemia, macroamylasemia, and a markedly increased amylase clearance/creatinine clearance ratio in a patient with renal cell carcinoma. Serum amylase activity was characterized as macroamylase by gel exclusion chromatography. Electrophoretic separation revealed an atypical band of amylase, migrating anodal to the S2 control fraction. Electrophoresis of urine revealed the presence of both S1 and S2 fractions, but not the atypical band found in serum. Quantification of the salivary- and pancreatic-type amylase fractions showed amylase in urine to be 100% salivary. Immunofixation disclosed the macroamylase to consist of an immune complex between amylase and IgA-lambda antibody. Binding-capacity studies showed that the serum immunoglobulin was present in excess and could bind 46% and 49% additional S-type amylase activity derived from saliva and the patient's urine, respectively. The amylase clearance/creatinine clearance ratio was markedly supranormal (0.134), unexpected in a patient with macroamylasemia. A biopsy specimen of the renal cell tumor was found to contain significant salivary-type amylase activity. These results suggest production of amylase by tumor tissue in the renal carcinoma and secretion of S-type amylase into the patient's urine. Evidently, macroamylase should be confirmed by gel exclusion chromatography.

Aged↗
PubMed1989

[Evaluation and determination of P-type-alpha amylase activity in human serum by monoclonal antibody].

We evaluated a kinetic procedure for determining pancreatic type of alpha-amylase isoenzyme (EC 3.2.1.1.) by using monoclonal salivary amylase antibody in human serum. The principle of this method is to measure residual pancreatic amylase activity after the reaction of monoclonal anti-salivary amylase antibody which is specifically inactivated human salivary amylase. The reaction of antibody with salivary alpha-amylase completed within 2 min of incubation and residual activity of pancreatic amylase was 100%, and the residual salivary amylase activity showed less than 3% of salivary amylase activity after incubation with antibody. The reproducibility and/or precision was 1.2% to 3.4% and the linearity obtained up to 1.500 U/l. Correlation coefficient between the proposed method (y) and electrophoresis (x1) and wheat germ inhibition method (x2) was well, respectively (r = 0.99 with both method, the regression curves was y = 1.02 x1-0.7 and y = 1.04x2-0.7). The reference value from healthy adults (male 98 and female 102) showed 13.6-48.2 U/l according to statistical parametric method and sex difference was not observed. The monoclonal anti-salivary amylase antibody was not cross-reacted with the other animal serum salivary type of amylase.

Animals↗
PubMed1979

Effect of pancreatic stimulation on serum and urine amylase isoenzymes in man.

Alpha amylase of pancreatic origin is cleared by the kidney more rapidly than the salivary isoamylase. To determine whether alterations in the ratio of pancreatic to salivary amylase in sera caused alterations in over all renal clearance, the clearance of amylase was measured before and after the exocrine pancreas was stimulated with a prolonged intravenous infusion of secretin plus cholecystokinin. Serum and urine samples collected prior to and following stimulation were analyzed for amylase activity and creatinine concentration. Amylase isoenzymes were separated using isoelectric focusing. Over all renal clearance of amylase and of the separated amylase isoenzymes were calculated as a percentage of the clearance of creatinine. The hormone infusion was associated with an increase in serum and urine amylase activities, this increase being mainly accounted for by pancreatic amylase. The renal clearance of the salivary and pancreatic isoamylases was not altered by the hormone infusion but the over all amylase clearance by the kidney rose from 2.31 +/- 0.74 to 3.42 +/- 1.46% of creatinine clearance. In some cases the renal clearance of amylase following stimulation entered the range considered diagnostic for acute pancreatitis.

Amylases↗
PubMed1984

Isoproterenol-induced amylase release in rabbit parotid acini: relation of protein phosphorylation, cyclic AMP and related kinase activity to changes in secretory rate.

Isoproterenol-induced amylase release from rabbit parotid acini was examined in relation to cyclic AMP (cAMP) concentrations, cAMP-dependent protein kinase (cAMP-PK) activity ratios and protein phosphorylation. Initial stimulation of amylase release by isoproterenol was preceded by increases in cAMP, cAMP-PK activity ratios and phosphorylation of a 34,000 MW (major) and a 30,000 MW (minor) protein in the microsomal fraction. When propranolol was added, decreases in cAMP concentrations and cAMP-PK activity ratios preceded the reduction in amylase release. Detailed analysis was performed on the 34,000 MW protein. The relation of dephosphorylation of protein 34 and reduction in amylase release was complex. Slight dephosphorylation occurred before or concurrently with the decrease in amylase release; however, maximal dephosphorylation was preceded by maximal inhibition of amylase release. When secretion of amylase was reinstituted by isoproterenol or forskolin, increases in cAMP and cAMP-PK activity ratios occurred before or in concert with amylase release but rephosphorylation of protein 34 occurred after the start of amylase release. Photoaffinity labeling studies using [32P]-8-azidoadenosine-3',5'-cyclic monophosphate indicated that proteins 34 and 30 were not regulatory subunits of cAMP-PK or their breakdown products. Although these data are consistent with phosphorylation of proteins 34 or 30 being required for triggering initial secretion, maximum dephosphorylation was not essential for inhibition of secretion. Furthermore, initiation of amylase release by the gland after a short period of quiescence did not depend on prior phosphorylation of protein 34. These data may indicate the absence of a requirement of amylase release for phosphorylation of protein 34.

Adenosine Triphosphate↗
PubMed1976

Amylase isoenzyme clearances in normal subjects and in patients with acute pancreatitis.

Renal clearances of amylase isoenzymes, expressed as percentages of creatinine clearances, were determined in 20 normal subjects and in 8 patients with acute pancreatitis. The isoenzyme assay employed thin layer isoelectric focusing, starch iodine staining, and densitometry. Normal clearance of pancreatic-like amylase (mean +/- SE: 3.00 +/- 0.40%) was greater than the clearance of salivary-like amylase (0.51 +/- 0.06%) in ea ch individual (P less than 0.001). However, the amount of pancreatic amylase in the serum was not the major determinant of amylase clearance. Normal clearance of pancreatic-like amylase was significantly (P less than 0.001) less than the clearance of total serum amylase in acute pancreatitis (6.49 +/- 1.07%). In pancreatitis the clearance of pancreatic-like amylase (7.29 +/- 1.19%) and the clearance of salivary-like amylase (4.55 +/- 1.02%) were both elevated compared to normal (P less than 0.001). These findings indicate that the increased clearance of amylase in pancreatitis results from a change in renal function rather than a change in serum amylase. Renal changes not reflected by increased serum creatinine or more than mild proteinuria may be manifestations of the systemic toxicity of acute pancreatitis.

Acute Disease↗