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At least 1,531 records · Page 85Linked to original sources
PubMed1985

Alterations in serum pancreatic elastase 1 content in acute and chronic pancreatitis: comparison with alpha-amylase activity.

Serum pancreatic elastase 1 content in 45.9% of 203 samples from 32 patients with acute pancreatitis was found to be greatly elevated to greater than 1000 ng/dl, much higher than the control values (90 to 270 ng/dl), whereas serum alpha-amylase activity, in 62.3% of the same samples, was within the control range (100 to 460 IU/L). The increased pancreatic elastase 1 content persisted for several days after serum alpha-amylase activity returned to normal, suggesting that, compared with serum alpha-amylase activity, pancreatic elastase 1 content truly reflects the clinical course of acute pancreatitis. The measurement of pancreatic elastase 1 content appears to be more valuable in the diagnosis and prognosis of acute pancreatitis than that of serum alpha-amylase activity. In 41 patients with chronic pancreatitis, on the other hand, pancreatic elastase 1 content and serum alpha-amylase activity were within the normal range in 38.3% and 56.2% respectively, of 336 samples.

Acute Disease↗
PubMed1985

Specific immunoassay of alpha-amylase isoenzymes in human serum.

A monoclonal antibody (66C7) was prepared that specifically binds human salivary amylase (EC 3.2.1.1); it cross reacts with human pancreatic amylase by less than 1%. Two procedures are described for determination of isoamylases in human serum with this antibody: an enzyme immunoassay for determining amylase of salivary origin, and a routine method in which this amylase is immunoprecipitated and the remaining (pancreatic) amylase activity is assayed. Results by the two methods correlate well.

Antibodies, Monoclonal↗
PubMed1980

Aging changes of pancreatic isoamylases and the appearance of "old amylase" in the serum of patients with pancreatic pseudocysts.

Human serum and pancreatic secretions contain at least three isoamylases of pancreatic origin. As determined by gel electrophoresis and saccharogenic amylase assay, P1, P2, and P3 designate isoenzymes with slow, intermediate, and rapid electrophoretic mobilities, respectively. The P1 isoamylase normally accounts fo 80-90% of total amylase activity, P2 for 10-20%, and P3 for 0-4% in both serum and pancreatic juice. When pancreatic amylase is incubated at 37 degrees C, P1 decreases, and P2 and P3 increase within hours. Whereas P2/P1 is always < 0.25 in fresh pancreatic juice, normal serum, acute pancreatitis serum, chronic pancreatitis serum, or pancreatic cancer serum, the ratio was elevated in 11 of 12 pseudocyst contents (mean P2/P1 = 0.51) and in 14 of 16 sera from patients with proven pseudocysts (mean P2/P1 = 0.43) (P < 0.001). After pseudocysts were surgically drained, the proportions of the pancreatic isoamylases in serum reverted to normal. The precise, characteristic, and predictable changes in electrophoretic mobility, presumably a result of specific spontaneous chemical alterations of the isoenzyme molecules, allow identification of "old amylase" in the serum of patients with pancreatic pseudocysts. This finding may be a useful adjunct for diagnosis, but whether the amount of "old amylase" can be used to estimate the age of a pseudocyst is not yet known.

Acute Disease↗
PubMed1980

P3 amylase isoenzyme in the diagnosis of pancreatitis.

P3 amylase isoenzyme was found to be present in the plasma of 43 out of 140 patients with suspected pancreatitis. Of 43 patients with the P3 isoenzyme, pancreatitis was definitely confirmed in 21 by laparotomy. Of the remainder, 19 had probable pancreatitis based on a combination of clinical, biochemical, endoscopic (ERCP), ultrasonic and computerised tomographic evidence, while 3 had possible pancreatitis based on clinical evidence alone. Of 97 patients without the P3 isoenzyme 1 patient had evidence of probable pancreatitis and 1 had evidence of possible pancreatitis. Statistical analysis (excluding the 4 cases of possible pancreatitis) showed that the P3 amylase isoenzyme had a sensitivity of 98%, a specificity of 100% and an efficiency of 99%. The predictive values of a positive and negative test were 100% and 99% respectively. Hyperamylasemia was not a pre-requisite to the presence of the P3 isoenzyme, since 11 out of 13 patients, with normal total amylase levels, were found to have the P3 band and confirmation of their pancreatitis. It is concluded that the P3 amylase isoenzyme is a specific and sensitive test for pancreatitis, and appears also to be superior to the total plasma amylase.

Acute Disease↗
PubMed1981

Physiological studies on Phymatotrichum omnivorum. XII Influence of cultural conditions on amylase synthesis.

The production of extracellular amylase by P. omnivorum has been studied under different cultural conditions. Maximum mycelial growth and amylase synthesis were found in basal synthetic medium containing 2% glycogen as the carbon source. Significant amounts of amylase and growth were obtained in medium containing other carbon compounds with alpha-1, 4-linkages. Optimum temperatures for mycelial growth and amylase synthesis were found at 28 degree and 30 degree C, respectively. Of all the nitrogenous compounds tested, ammonium nitrate supported the maximum mycelial growth and amylase production. Increasing the concentration of starch in the basal medium increased the growth as well as the enzyme synthesis.

Amylases↗
PubMed1982

[Degradation of inactivated alpha-amylase by associated proteases].

Alpha-Amylase preparations often contain small quantities of proteolytic activity which are difficult to remove. On the example of fungal alpha-amylase, such associated proteases have been shown to possess a specific activity to the denatured amylase molecules. The amylase is not attacked under native conditions, whereas in the thermal denaturation a rapid degradation of only the inactivated molecules occurs. A specific metabolic function of these associated proteases in the return of denatured amylase molecules to the amino acid pool is suggested.

Amylases↗
PubMed1983

Variations in amylase isoenzymes and lipase during acute pancreatitis, and in other disorders causing hyperamylasemia.

We compare the clinical value of assay of amylase (EC 3.2.1.1) isoenzymes with that of lipase (EC 3.1.1.3) in serum from patients with proven acute pancreatitis or with hyperamylasemia from other causes. In the former group we measured amylase, lipase, and isoamylases daily. Lipase and P(pancreas)-type isoamylases reached the highest mean values on the first day of an attack of acute pancreatitis (day one). Lipase declined rapidly, and by day four its mean activity was about the same as that of amylase and lower than that of the P-type isoamylases. Great inter-individual variations were found among patients with a similar clinical course. Of the 85 samples analyzed, amylase activity for 36 declined to within reference limits, but 18 of the 36 had high lipase activity, 18 had high P-type isoamylases activity, and 31 had P3 isoenzyme, which is not detectable in normal sera. Determination of isoamylases is a more sensitive index to acute pancreatitis than lipase assay and may be particularly useful when pancreatitis is suspected despite a normal total amylase activity. In the group of patients with hyperamylasemia from other origins, three had macroamylasemia, one had mumps, one had abdominal trauma without pancreatic injury, and one had pelvic inflammatory disease. The specific pattern of macroamylase on electrophoresis permitted a precise diagnosis of macroamylasemia; normal lipase had only ruled out pancreatitis. In the three other cases, lipase and isoamylases excluded pancreatic involvement.

Acute Disease↗
PubMed1984

Independent regulation of nonallelic pancreatic amylase genes in diabetic mice.

Administration of streptozotocin produces a diabetic condition in mice characterized by a specific decrease in amylase synthesis in the pancreas as well as a substantial reduction in amylase mRNA concentration. We have studied this effect in mice of the congenic strains C3H.AmyYBR and C3H.AmyCE with multiple active copies of the pancreatic amylase structural gene. When mice of these strains are treated with streptozotocin, the magnitude of reduction in the synthesis of each amylase isozyme is different. These differences are reflected in the relative activities of isozyme-specific mRNAs in an in vitro translation assay. Administration of insulin results in partial restoration of normal phenotypes. The results provide genetic evidence that individual copies of the amylase structural gene are associated with divergent cis-acting insulin-responsive sequences.

Alleles↗
PubMed1984

The role of calcium and cyclic AMP in amylase release from isolated rat parotid acinar cells: effect of calcium ionophore A23187.

The effect of the Ca ionophore A23187 on isoproterenol (ISP)-induced amylase release was investigated using isolated rat parotid acinar cells. A23187 increased amylase release in normal medium but this stimulated effect of A23187 was abolished in Ca-free medium. ISP-induced amylase release was inhibited by A23187 in Ca-free medium but not in normal medium. A23187 did not affect basal levels of cyclic AMP in normal medium or Ca-free medium but reduced the accumulation of cyclic AMP stimulated by ISP in both mediums. Both NaF- and ISP-stimulated activities of adenylate cyclase were reduced in washed membrane fraction prepared from A23187-treated slices of parotid glands. 45Ca2+ uptake stimulated by A23187 markedly increased, reached maximum at 10-20 min and then declined immediately. These results suggest that A23187 decreases the accumulation of cyclic AMP stimulated by ISP and results in an inhibition of ISP-induced amylase release in the absence of extracellular Ca2+, whereas a marked influx of Ca2+ stimulated by A23187 may possibly compensate the decrement of amylase release in the presence of extracellular Ca2+.

Adenylyl Cyclases↗
PubMed1984

Structural genes for alpha-amylases are located on barley chromosomes 1 and 6.

Genomic DNA from six euplasmic wheat-barley addition lines and from the wheat and barley parents were analyzed for the presence of alpha-amylase gene sequences, using plasmid DNAs from two different alpha-amylase cDNA clones as hybridization probes. Barley-specific alpha-amylase gene sequences were detected only in addition lines 1 and 6 carrying barley chromosomes 1 and 6, respectively. One cDNA clone probe hybridized strongly to sequences on chromosome 6 but not to those on chromosome 1. The other cDNA clone probe preferentially hybridized to sequences on chromosome 1. It is concluded that structural genes for alpha-amylases are located on barley chromosomes 1 and 6. alpha-Amylase genes on the same chromosome appear to be closely related to one another but substantially different from those on the other chromosome.

Chromosome Mapping↗
PubMed1984

A complementary DNA sequence that predicts a human pancreatic amylase primary structure consistent with the electrophoretic mobility of the common isozyme, Amy2 A.

We report the nucleotide sequence of mRNA for the common electrophoretic isozyme of human pancreatic alpha-amylase, Amy2 A. The sequence was derived from a nearly full-length complementary DNA (cDNA) isolated from a cloned cDNA library. The relatively short 5' untranslated region (15 nucleotides) was determined by primer-extension sequencing. The human Amy2 messenger codes for a 511-residue preamylase polypeptide. An amino-terminal signal peptide of 15 amino acids with an Ala X Gln cleavage site is proposed based on homology to mouse, dog and hog amylases. The Amy2 A mRNA sequence differs from a recently reported human Amy2 sequence. Differences were found at 31 nucleotide positions. The alpha-amylase proteins predicted by the two mRNAs differ at 17 amino acid positions. Relative to the known sequences of other mammalian amylases, most of the differences between the two human Amy2 sequences appear to have occurred as substitutions in the sequence reported by Nakamura et al. (1984). These substitutions predict a protein with a substantially greater net negative charge than that of Amy2 A. We suggest that the two sequences may represent either divergent Amy2 alleles or the expression of non-allelic pancreatic amylase genes.

Amino Acid Sequence↗
PubMed1978

Amylase elevation attributable to an ovarian neoplasm.

An ovarian carcinoma producing amylase-rich ascites and pleural effusions is reported; salivary type amylase was identified in tumor tissue. A variety of nonpancreatic diseases and tumors of lung, parotid, ovary, and other organs have been associated with elevated amylase in serum or body fluids. Amylase isoenzyme electrophoresis is of value in differentiating pancreatic from nonpancreatic sources of increased amylase.

Aged↗
PubMed1983

Correlation between alpha-amylase production and sporulation in Bacillus licheniformis CUMC 305 with respect to the effect of some carbohydrates and phenylmethylsulfonyl fluoride treatment.

The existence of any relationship between extracellular alpha-amylase production and sporulation in Bacillus licheniformis CUMC 305, when grown in the presence of different carbohydrates, was investigated. It was noted that alpha-amylase production in the organism was almost complete during the period of maximum sporulation, irrespective of the carbon source used. The effect of a sporulation inhibitor, phenylmethylsulfonyl fluoride at a concentration of 8 micrograms/ml, on enzyme secretion was an interesting feature. It was observed that alpha-amylase production as well as sporulation deteriorated, if the inhibitor was added to the external growth medium during the period extending from mid-logarithmic phase to mid-stationary phase of the growth cycle; contrary to it, there was no change in the pattern of alpha-amylase production or sporulation when added either earlier or later than this period. It may be concluded that the extracellular pool was the principal yield of alpha-amylase in the organism, since washing experiments and subsequent treatment of the intact cells with Tris hydroxymethyl aminomethane hydrochloride buffer or lysozyme, surfactant (Tween-80), or lysozyme-Tween mixture failed to extricate any substantial quantities of the enzyme. The intracellular pool of enzyme, obtained by disrupting the cells, was insignificant compared to the extracellular pool.

Bacillus↗
PubMed1978

Serum values of amylase and pancreatic lipase in healthy mature dogs and dogs with experimental pancreatitis.

Serum values of amylase and pancreatic lipase were determined by the iodometric and the turbidimetric methods, respectively, in 44 mature healthy dogs and in 8 dogs with experimentally induced pancreatitis (plus 1 sham-operated control). Serum value of amylase in mature healthy dogs varied from 250 to 1,500 Caraway units/dl and that of pancreatic lipase varied from 0 to 50 IU/L. Maximal serum values of amylase and pancreatic lipase in the dogs with experimentally induced pancreatitis varied from 4,540 to 14,000 Caraway units/dl and 325 to 810 IU/L, respectively. Following pancreatic damage, serum values of amylase and pancreatic lipase increased rapidly in the 8 dogs and ran parallel to each other in 6 of the 8 dogs studied. However, the serum value of amylase returned to within normal range earlier than the serum value of pancreatic lipase in 2 dogs; the reverse was true in 2 other dogs.

Amylases↗
PubMed1978

[Significance of the determination of multiple forms of urinary amylases for the diagnosis of exocrine pancreas diseases].

The multiple amylases of the urine were examined in healthy persons and in patients with acute and chronic pancreatitis as well as with parotitis using the polyacryl amide gel disk electrophoresis. A separation into about 7 amylase-containing fractions was achieved which could be coordinated to the pancreatic juice and to saliva. In acute pancreatitis the pancreas amylases increased, in chronic pancreatitis, on the other hand, they decreased. In parotitis the salivary amylases increased. For diagnostic purposes the formation of quotients from certain fractions was useful. The examination of the multiple amylases of the urine according to the method mentioned leads to an improved clinico-chemical diagnostics of diseases of the exocrine pancreas and gives the possibility of their course control.

Acute Disease↗
PubMed1977

[Formation of high-molecular aggregates between serum amylase and colloidal plasma substitutes (author's transl)].

The distribution of molecular weights of human serum amylase was studied by gel filtration of serum, obtained before and after infusion of the colloidal plasma substitutes hydroxyethyl starch, dextran and gelatin, respectively. Both in serum, drawn after intravenous infusion of hydroxyethyl starch, and in a solution of hydroxyethyl starch with serum we observed a significant increase in the molecular weight of serum amylase. The occurrence of this "macroamylase" may be explained by the formation of aggregates between hydroxyethyl starch and amylase. Because of its high molecular weight the elimination of this, presumably, enzyme-substrate-complex is retarded, thus leading to the observed increase of serum amylase activity. In contrast to these observations concerning hydroxyethyl starch no change in the apparent molecular weight of serum amylase was observed following the infusion of either gelatin or dextran or their solutions with serum.

Amylases↗
PubMed1994

The activity of granulocyte alpha-amylase in acute appendicitis.

The activity of alpha-amylase was measured in isolated granulocytes, serum and urine of 35 patients with acute appendicitis. The measurements were performed before operation and on the 7th day after operation. Slightly increased activity of alpha-amylase was found in the serum and urine of 15 patients. On the 7th day after operation the activity of this enzyme reached normal value. The activity of granulocyte alpha-amylase was elevated in 22 patients. In 2 of them the increased activity still maintained on the 7th day after operation. Positive correlation between the serum and granulocyte alpha-amylase activities was found. These observations allow to conclude that granulocytes are the source of increased alpha-amylase activity in the serum of patients with acute appendicitis.

Adolescent↗
PubMed1994

Amylase in lung carcinomas. An ultrastructural and immunohistochemical study of two adenocarcinomas, and a review of the literature.

The ultrastructure of two lung adenocarcinomas with immunohistochemical and biochemical expression of amylase is reported. Isoenzyme determination performed on tumour tissue showed a salivary-type amylase. None of the carcinomas was associated with hyperamylasaemia. Ultrastructurally, the adenocarcinomas contained a varying number of heterogeneous granules resembling lysosomes. None of the tumours contained mature zymogen granules. The findings are discussed in relation to previous cases of amylase-containing lung carcinomas subjected to electron microscopy. The vast majority of these carcinomas were associated with a significant elevation of serum amylase. Various theories which might explain the absence of hyperamylasaemia in the presented cases are proposed. The biological and diagnostic significance of amylase production is discussed.

Adenocarcinoma↗