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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The alpha-amylases from five strains of Bacillus amyloliquefaciens were compared to determine whether differences in primary structure are responsible for variations in catalytic properties previously reported among the enzymes. Amino acid analysis established virtually identical compositions for the proteins. Reaction with dimethylaminoaphthylene sulfonylchloride indicated the amino-terminal amino acid of each amylase to be valine. Carboxyl termini of the enzymes have been determined by digestion with carboxypeptidase A. The resulting kinetic data indicate tyrosine as the carboxyl terminus and leucine as the penultimate residue for all five proteins. Isoelectric focusing of the enzymes yielded isoelectric points in the pH range of 5.09 to 5.18. Tryptic digests of the enzymes chromatographed on a cation-exchange column showed identical elution patterns. It is concluded that the primary structure of the amylase from the five strains is identical or exhibits only conservative substitutions.
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PMID:alpha-amylase from five strains of Bacillus amyloliquefaciens: evidence for identical primary structures. 30 94

Agarose gel electrophoresis (at pH 8.6) was used for qualitative determination of pancreatic enzymes in duodenal juice. The various enzymes were identified by staining techniques with specific chromogenic substrates, by quantitative determination of enzymes in eluates of gel slices, and by immunoelectrophoresis. The various protein bands corresponded to the following enzymes (from the anode to the cathode): chymotrypsin, trypsin, carboxypeptidase A, chymotrypsin, amylase (around the slit), lipase, elastase, and trypsin. The method was applied to a study of exocrine pancreatic function in 10 adults and 83 children suspected of having malabsorption. The duodenal juice, also analyzed for trypsin and amylase content, was collected in fasting condition and after a test meal of water. In patients with normal pancreatic function, all the enzyme bands were present and easy to recognize. In 87 patients carboxypeptidase A was present as two bands in 68 (80%), anodal trypsin as two bands in 39 (45%), and cathodal trypsin as two bands in 85 (97%). Electrophoresis of duodenal juice gave as much information from the fasting sample as after the test meal. Six children with pancreatic insufficiency (cystic fibrosis and Shwachmar's syndrome) had no or only faintly stained enzyme bands and a strongly stained albumin-containing band most anodally. The method is simple, rapid, and useful in routine work. The combination of this qualitative test with a quantitative one (e.g. trypsin determination) provides good information about exocrine pancreatic function.
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PMID:Agarose gel electrophoresis of duodenal juice in normal condition and in children with malabsorption. 43 37

Studies on the identification of the terminal residues in protease-free hog pancreatic alpha-amylase, prepared by glycogen precipitation, demonstrated the absence of free amino terminals when four different chemical procedures were used. These methods were based on reaction with fluorodinitrobenzene, trinitrobenzenesulfonic acid, dansyl chloride, and cyanate. In the search for the presence of a possible alpha-N-blocking group, an acetyl group was detected as acetic acid dinitrophenyl hydrazide after hydrazinolysis and dinitrophenylation. Quantitation of acetyl groups by a gas chromatographic or a specific enzymatic method yielded 0.7 mol of acetyl group per 51,000 g of protein. Other acyl groups, such as formyl or propionyl, were not found. Leucine was shown to be the carboxyl terminal residue by hydrazinolysis or by carboxypeptidase A digestion of acid denatured amylase. With either procedure, 0.8 mol of carboxyl terminal leucine was found per 51,000 g of protein. These findings are consistent with the proposal that hog pancreatic alpha-amylase is composed of a single, alpha-N-acetylated chain of molecular weight 50,000. Claims of other investigators for subunit and multichain structures for this enzyme are discussed in view of these end group data.
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PMID:Terminal residues of hog pancreatic amylase. 98 1

The presence of the enzymatically active allergens equivalent to Der p I (cysteine protease), Der p III (serine protease) and amylase in extracts of Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei was determined using appropriate enzymatic techniques. Biochemical equivalents of all three allergens were present in each extract studied. Studies also showed that the mite extracts contained a variety of other biochemically active enzymes including trypsin, chymotrypsin, carboxypeptidase A and B, glucoamylase and lysozyme. Marked differences in the relative concentrations of some of these enzymes in different mite extracts were observed, particularly trypsin and carboxypeptidase A. The enzymes were physicochemically similar to equivalent enzymes from vertebrate and invertebrate sources. Chromatofocusing studies of faecal extracts derived from D. pteronyssinus and D. farinae showed that several isoforms of each enzyme were present. The data indicated that there were more trypsin isoforms, with pI over a wider range, in extracts prepared from D. pteronyssinus. Proteases and carbohydrases were also found in extracts prepared from faecally enriched material suggesting that they were endoperitrophic and associated with mite digestion. The data suggest that not only are the group I, III and amylase allergens a consistent feature of most pyroglyphid dust mites but also that other proteases and carbohydrases present in mite faeces are allergenic.
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PMID:A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei. 128 68

The immunocytochemical detection of amylase, carboxypeptidase A, alpha 1-antitrypsin, carcinoembryonic antigen (CEA) and keratin in normal canine pancreatic tissue and in carcinomas of the exocrine pancreas of the dog is described. In the normal pancreas, the acinar cells contain amylase, carboxypeptidase and alpha 1-antitrypsin. The pancreatic ducts react with the antikeratin antibody. Twelve out of 14 pancreatic exocrine carcinomas showed immunoreaction with antiamylase antibody, and 10 with anticarboxypeptidase antibody. Five neoplasms reacted with anti-CEA antibody and three with the anti-alpha 1-antitrypsin antibody. It was not possible to find any systematic difference in the immunocytochemical profiles of acinar, tubular and undifferentiated carcinomas. These results indicate that immunocytochemical marking of amylase and carboxypeptidase is of value in the diagnosis of pancreatic neoplasms in the dog, especially if metastasis is the only material available for study and the tumour does not show any diagnostic feature on routine light microscope preparations.
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PMID:Immunocytochemical detection of amylase, carboxypeptidase A, carcinoembryonic antigen and alpha 1-antitrypsin in carcinomas of the exocrine pancreas of the dog. 137 27

The effect of dietary protein on enzyme activity of pancreatic juice was studied in ten growing, castrated, Large White male pigs. Animals, fitted with permanent cannulas in the pancreatic duct and in the duodenum, were divided into two groups receiving either casein or rapeseed concentrate as a protein source. After a 15 d adaptation period to the experimental diet, the volume of pancreatic secretion was significantly higher, whereas the protein concentration was lower in the casein group compared with the rapeseed group. No statistical difference was observed in the daily protein output between groups. Total secreted activities of carboxypeptidase A (EC 3.4.17.1), and elastase (EC 3.4.21.36) were higher in the casein group during the nocturnal period, whereas total activities of trypsin (EC 3.4.21.4), chymotrypsin (EC 3.4.21.1), carboxypeptidase B (EC 3.4.17.2) and amylase (EC 3.2.1.1) in pancreatic secretions during the post-prandial periods were increased by the ingestion of the rapeseed diet. It is concluded that the pancreatic enzyme secretion is sensitive to the nature of the protein ingested.
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PMID:Effects of diets containing casein and rapeseed on enzyme secretion from the exocrine pancreas in the pig. 137 39

Pancreatic juices were collected by selective reverse catherism of the chief pancreatic duct in two patients, one free from pancreatic disease and the other having a pancreas cancer. They were analysed in detail especially in order to get information on the mechanism of enzyme excretion. The variations of the digestive enzyme activities (amylase, lipase, trypsin, chymotrypsin, carboxypeptidase A and B) were not superimposable among them or with the fluctuations of the protein concentration in the pancreatic juice samples. These results agree with a non-parallel enzyme-excretion mechanism by the pancreas. However deep electrophoresis analyses of pancreatic juice samples showed that the ratio of each digestive enzyme concentration remained almost constant in the same patient. This observation disagrees with the above conclusion and suggests that the data obtained by using classical methods for estimating digestive enzyme activities have to be considered prudently. By another way, two main significant differences were reported by analysing the ionic composition of the pancreatic juice samples following their origin. The pancreatic juice samples of the patient having a pancreas cancer had a lower and more variable Na+ concentration than those coming from the patient who was free from pancreas disease. They had a HCO3- concentration which was almost constant, contrary to what was observed for the pancreatic juice secreted by the other patient.
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PMID:[Detailed analysis of human pancreatic secretions collected by retrograde catheterization. Parallel or non-parallel excretion of digestive enzymes?]. 138 69

The appearance and activity of various porcine pancreatic hydrolases were studied during fetal and postnatal development. Quantitatively, the enzyme activities in activated pancreas homogenates were low but increased during the second half of the fetal period, using the substrates Bz-Arg-pNA for measuring anodal and cathodal trypsin, Suc-Phe-pNA (chymotrypsin A and C, and elastase II) and Suc-(Ala)3-pNA (elastase I and protease E). Postnatally, after an initial decrease during the first week, the enzyme activities increased markedly, especially from 10-14 weeks to 6 months. The individual hydrolases were identified after electrophoretic separation in agarose gel and staining with various substrates either directly in the gel or after transfer to nitrocellulose membranes (enzymoblotting). During the fetal period, chymotrypsin A and B, elastase II, carboxypeptidase A, and amylase appeared at approximately 65 days and anodal trypsin, at approximately 76 days. After birth, new proteinases appeared after the first week including chymotrypsin C, cathodal trypsin, and protease E, whereas elastase I was found from 5 weeks after birth. Concomitantly, unidentified "fetal proteinase(s)" with caseinolytic, Ac-Phe-beta NE and CBZ-Ala-beta NE activities began to diminish and disappeared 10-14 weeks after birth. This study showed a marked increase in the overall pancreatic enzyme activities, as well as an age-dependent expression of the variety of pancreatic hydrolases during porcine ontogeny.
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PMID:Development of porcine pancreatic hydrolases and their isoenzymes from the fetal period to adulthood. 244 72

This adaptation of a commercially available kit for automated measurement of carboxypeptidase A (CPA; EC 3.4.17.1) activity in serum with the Cobas Bio centrifugal analyzer extends the linear range to an activity concentration of 82 U/L. Results obtained by the described method correlated closely (r = 0.98) with those by the manual kit method. The reference interval for 150 apparently normal individuals was 0.12-0.91 U/L. Total CVs of the method ranged from 4.0% to 13.1%. Bilirubin and glucose decreased the CPA activity in serum by as much as 98% and 26%, respectively. Substantial CPA activity was found in pancreatic tissue, with little activity in intestinal tissue. CPA activity was not as widely distributed in extra-pancreatic tissues as were amylase and lipase activities. Peak activities of CPA, amylase, and lipase in the sera of patients with acute pancreatitis were significantly correlated (r = 0.45 to 0.78, P less than 0.05-0.01). The optimized diagnostic efficiency of CPA for acute pancreatitis was 0.85 at a cutoff value of 5 U/L. Amylase and lipase exhibited similar optimized efficiencies, and parallel testing did not significantly improve diagnostic accuracy. We conclude that automated analysis for CPA activity, even in the absence of interferences, does not add to the diagnostic information provided by the widely available assays for amylase and lipase activity.
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PMID:Measuring carboxypeptidase A activity with a centrifugal analyzer: analytical and clinical considerations. 246 45

Footprint analysis of the 5'-flanking regions of the alpha-amylase 2, elastase 2, and trypsina genes, which are expressed in the acinar pancreas, showed multiple sites of protein-DNA interaction for each gene. Competition experiments demonstrated that a region from each 5'-flanking region interacted with the same cell-specific DNA-binding activity. We show by in vitro binding assays that this DNA-binding activity also recognizes a sequence within the 5'-flanking regions of elastase 1, chymotrypsinogen B, carboxypeptidase A, and trypsind genes. Methylation interference and protection studies showed that the DNA-binding activity recognized a bipartite motif, the subelements of which were separated by integral helical turns of DNA. The alpha-amylase 2 cognate sequence was found to enhance in vivo transcription of its own promoter in a cell-specific manner, which identified the DNA-binding activity as a transcription factor (PTF 1). The observation that PTF 1 bound to DNA sequences that have been defined as transcriptional enhancers by others suggests that this factor is involved in the coordinate expression of genes transcribed in the acinar pancreas.
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PMID:Identification of a cell-specific DNA-binding activity that interacts with a transcriptional activator of genes expressed in the acinar pancreas. 278 41


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