Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Six pigs, initially of 35 kg mean live weight, were each fitted with a re-entrant cannula. This was formed on either side of a short pouch of duodenum into which the pancreatic duct opened and which contained a simple cannula linked to the centre of the re-entrant cannula. Each pig received two diets: diet A was based on wheat starch, sucrose and casein, while diet B was based on barley and soya-bean meal. The diets were given in equal amounts at 12 h intervals. Digesta and pancreatic juice were collected continuously during three 12 h periods for each pig on each diet. Mean duodenal output: dietary intake values for diets A and B respectively were: digesta 1.80, 2.86; dry matter 1.05, 1.03; nitrogen 1.05, 1.06; trichloroacetic acid (TCA)-soluble N 7.69, 9.10; glucose 0.97, 0.89. For diet A the proportion of TCA-soluble N in total N rose from 13 to 50% during 12 h, while it was approximately 50% throughout 12 h for diet B. Mean total pepsin (EC 3.4.23.1) activities (units/24 h) were 760449 (diet A) and 1 466 571 (diet B). Salivary and gastric secretions were calculated to be approximately 4 and 8 kg/24 h for diets A and B respectively. Mean flows in pancreatic juice (g/24 h) for diets A and B respectively were: juice 1204, 2182; protein 10.94, 12.10; N 1.98, 2.14; ash 9.46, 17.31; sodium 3.88, 6.91; potassium 0.23, 0.54; calcium 0.031, 0.046; phosphorus 0.024, 0.026. Mean total enzyme activities (units x 10(-3)/24 h) for diets A and B respectively were: trypsin (EC 3.4.21.4) 138, 114; chymotrypsin (EC 3.4.21.1) 84, 84; carboxypeptidase A (EC 3.4.2.1) 5, 4; carboxypeptidase B (EC 3.4.2.2) 15, 17; amylase (EC 3.2.1.1) 1061, 981. It was calculated that the minimum amount of endogenous N from saliva and gastric secretion was 0.3-0.6 g in 24 h. This assumes no absorption of N occurred anterior to the duodenal cannula.
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PMID:Studies on gastric digestion of protein and carbohydrate, gastric secretion and exocrine pancreatic secretion in the growing pig. 640 23

A marked proteolytic activity against casein can be demonstrated in rat liver mitochondria. The proteases degrading casein appear distributed between a sedimentable fraction (Po) and a soluble extract (So). Part of the soluble fraction activity, which may be recovered in the mitochondrial intermembrane space, results from a contamination by lysosomal proteases and can be eliminated by previously washing the mitochondria with digitonin. The pre-exposure to digitonin causes an enhancement of the caseinolytic activity associated with the membrane fragments, proving that this activity is not due to lysosomal enzymes. When rats have been injected in vivo with the compound 48/80 which, by degranulating the mast cells prevents contamination of the mitochondrial preparations by mast cell proteases, the membrane fraction (Po) retains a caseinolytic activity of the order of 80 per cent of the control preparations. A similar value of activity is observed in the membranes of brain mitochondria, isolated by a method which removes the rare mast cells they may contain. This shows that the greater part of the caseinolytic activity associated with the rat liver membranes does not originate from mast cell granules. Liver mitochondria pre-exposed to digitonin to eliminate lysosomal contaminants, have been subfractionated into matrix, intermembrane space, inner and outer membrane. Each of the fractions exhibits a caseinolytic activity, but the largest part is localized in the inner compartments of mitochondria: the matrix and the inner membrane. The optimal pH and the sensitivity to inhibitors of the proteases in the different compartments indicate that we are dealing with distinct enzymes.
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PMID:Study on the localization of proteases of mitochondrial origin. 681 21

Diets containing egg white, casein, menhaden fish meal, soy protein or wheat gluten were fed to rats to assess the impact of dietary protein (and other nutrients) on gastric functions. The menhaden fish meal group exhibited increases in stomach histidine decarboxylase (HDC) activity, histamine concentration, as well as acid secretion when compared with the control, casein group. When rats were fed amino acid-supplemented casein or fish meal diets to simulate each other's amino acid profile, a small increase in gastric HDC activity, histamine content and acid secretion was observed in comparison with the unsupplemented casein or fish meal groups. The high mineral content of menhaden fish meal (15%) was thought to be a potential inducing factor for gastric histamine metabolism and acid secretion. Adding fish meal ash to the casein diet or to a cod fillet diet elevated stomach HDC activity and histamine concentration significantly. Furthermore, when calcium (Ca) was added to the casein diet to simulate its high content in menhaden fish meal (7.8%), similar elevated levels of gastric histamine were obtained for the Ca-supplemented casein group as for the fish meal group. The role of Ca could be due to release of gastrin, which results in release of stomach histamine, or by facilitating mast cell histidine incorporation with subsequent histamine synthesis.
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PMID:Gastric histamine metabolism and acid secretion in rats as influenced by diet and nutrient content. 682 9

1. Pancreatic juice was collected from six pigs of 48 kg initial weight fitted with a collection catheter in the pancreatic duct and a return catheter in the duodenum. 2. Measurements of flow and composition of the juice were made during 24 h periods after adaptation to isonitrogenous diets based on barley, wheatings and fish meal (diet BWF) or starch, sucrose, casein, maize oil and cellulose (diet SSC), given in a change-over design. Measurements were also made during the periods of adaptation to a change from one diet to the other. 3. Mean flow-rates for pigs adapted to diets showed a highly significant four-fold difference between diets; values were 4962 ml/d for diet BWF and 1273 ml/d for diet SSC. The hourly volumes of juice were very variable and showed no clear response to feeding and no consistent diurnal pattern for either diet. 4. There were no significant differences between diets in the specific activities of the proteases. Average values were (units/mg protein) trypsin (EC 3.4.21.4) 29.6, chymotrypsin (EC 3.4.21.1) 7.7, carboxypeptidase A diet BWF than with diet SSC. The specific activities and total outputs of alpha-amylase (EC 3.2.1.1) and lipase (EC 3.1.1.3) were significantly higher for diet BWF than for diet SSC; specific activities for the two diets respectively were: (units/mg protein) alpha-amylase 95-6 and 42.3, lipase 59.0 and 14.5. 5. The higher daily volume of juice with diet BWF was associated with significantly (but only slightly) higher levels of both sodium and potassium, compared with diet SSC. 6. The results are discussed in relation to previous studies on digestion at this Institute, in which pigs with intestinal cannulas were given the same diets.
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PMID:The influence of diet on the exocrine pancreatic secretion of growing pigs. 704 29

The effect of increasing the flow of protein amino acids to the small intestine on the activities of pancreatic proteases and on the absorption site of amino acids was examined in sheep equipped with intestinal cannulas at 0.05, 11 and 25 m from the pylorus. A single concentrated diet providing 85.1 g of protein amino acids/day was fed throughout the experiment. During period 1 this was the only source of protein. During period 2, a suspension of casein was infused into the duodenum through the 0.05-m cannula at a rate of 100 g/day, which supplied to the small intestine a total of 177 g amino acids/day. In period 1, 56.7 g of amino acids was absorbed per day along the entire small intestine, and 85% of it was absorbed in the anterior 11 m. Of the 143 g of amino acids absorbed per day during period 2, 63% was absorbed in the anterior 11 m. Ninety-four percent of the infused casein was absorbed. Increasing the flow of amino acids to the small intestine of sheep from 85 to 177 g/day resulted in an overall elevation in the activities of chymotrypsin, carboxypeptidase A and trypsin at the 11-m site but not the 25-m site. The greatest increase was obtained with chymotrypsin: 119 and 114% for the specific and total activities, respectively, and the least with the trypsin: 38 and 36% for the specific and total activities, respectively.
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PMID:Effect of protein infused into sheep duodenum on activities of pancreatic proteases in intestinal digesta and on the absorption site of amino acids. 706 16

Carboxypeptidase A gamma from porcine pancreas was purified to homogeneity by ammonium sulfate fractionation, autolysis, batch absorption and elution from DEAF-Sephadex, and crystallization. The overall purification was about 32-fold with a yield of 31% and the specific activity of the purified protein was 108 units/mg protein. The apparent relative molecular mass determined by gel filtration on a Sephadex G-200 column was 38 900. The amino-terminal sequence of the porcine carboxypeptidase A gamma was Asn-Tyr-Ala-Thr-Tyr-His-Thr-Leu-Glu-Glu-Ile-Tyr-Asp-Phe-Met-Asp-Ile-Leu-Val-Ala -Glu-His-Pro-Gln-Leu- which was highly homologous to that of bovine carboxypeptidase A gamma. The purified enzyme was characterized with respect to isoelectric point (4.3). Km for N alpha-carbobenzoxyglycyl-L-phenylalanine (Cbz-Gly-LPhe) (20 mM), amino acid composition, pH optimum, pH stability, stability at different temperatures and effect of drying. The enzyme contained 1.01 mol zinc/mol and was inhibited by chelating agents such as EDTA and o-phenanthroline. Among substrates such as Cbz-Gly-LPhe, N alpha-benzoylglycyl-L-arginine, various kinds of amino acid esters, casein and elastin, porcine carboxypeptidase A gamma showed an enzymatic activity only towards Cbz-Gly-LPhe and casein. These data are in good agreement with the substrate specificity of bovine carboxypeptidase A.
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PMID:Crystallization and properties of carboxypeptidase A gamma from porcine pancreas. 727 15

The existence of a protein approximately 48% identical with mast cell tryptases was predicted previously from a dog mastocytoma cDNA. Antibodies raised against a peptide based on the deduced sequence suggested that the protein (dog mast cell protease-3, dMCP-3) is expressed in mast cells. In this report, characterization of the protein purified from mastocytomas reveals an N-glycosylated, high molecular weight, tryptic serine protease, which appears to be a tetramer of catalytic subunits, approximately half of which are linked by disulfide bonds. The oligomeric complex yields a single NH2-terminal sequence, which is identical with that predicted by dMCP-3 cDNA. This finding, and the lack of closely related genes on blots of genomic DNA, predict that each subunit is the product of one gene. Although dMCP-3 binds to heparin, it is active and stable at low ionic strength in heparin's absence. It resists inactivation by inhibitors in plasma but is sensitive to small inhibitors, e.g. leupeptin and bis(5-amidino-2-benzimidazolyl)methane (BABIM). dMCP-3 hydrolyzes extended peptidyl p-nitroanilides ending in basic residues, with P1 arginine preferred to lysine; it hydrolyzes the Arg18-Ser19 bond of calcitonin gene-related peptide but cleaves neither vasoactive intestinal peptide nor casein. These data suggest that dMCP-3 is a unique serine protease whose stability, formation of intersubunit disulfide bonds, inhibitor susceptibilities and substrate preferences differ from those of its closest relatives, the mast cell tryptases.
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PMID:Purification and characterization of dog mast cell protease-3, an oligomeric relative of tryptases. 776 12

In recent work we have shown that a serine proteinase, stratum corneum chymotryptic enzyme, with properties compatible with a role in desquamation in vitro as well as in vivo, is generally present in human stratum corneum. The enzymologic properties of the stratum corneum chymotryptic enzyme in a KCl extract of dissociated plantar corneocytes were compared with those of other known chymotryptic serine proteinases. Stratum corneum chymotryptic enzyme was found to differ significantly from bovine chymotrypsin, human cathepsin G, and human mast cell chymases in regard to inhibitor profile and substrate specificity. Stratum corneum chymotryptic enzyme was further purified from KCl extracts of dissociated plantar corneocytes by affinity chromatography on gels with covalently linked soybean trypsin inhibitor. The purified preparation contained one major component with apparent molecular weight 25 kD and one minor component with slightly higher apparent molecular weight as revealed by Coomassie staining after electrophoresis in polyacrylamide gels with sodium dodecyl sulphate of samples that had not been reduced. Both these components were associated with chymotrypsin-like activity as revealed by zymography in polyacrylamide gels with co-polymerized casein. On zymography gels, the purified preparation was also found to contain minor amounts of components with trypsin-like activity. The major purified protein had an apparent molecular weight of around 28 kD after reduction and full denaturation and was shown to contain carbohydrate.
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PMID:Purification and preliminary characterization of stratum corneum chymotryptic enzyme: a proteinase that may be involved in desquamation. 839 2

The practical application of exopeptidase has been limited by the high cost of the enzymes resulting from the low content of individual exopeptidase in the raw material. This can be overcome by the use of a combination of all the exopeptidases in the same enzyme source, as well as the use of the enzyme immobilization technology. A porcine pancreatic exopeptidase mixture was prepared by the ammonium sulfate precipitation at 35% saturation of the autolyzed pancreatic juice. The enzyme preparation was immobilized on thin shrimp chitin film by crosslinking with glutaraldehyde. The immobilized porcine pancreatic exopeptidases (IPPE) was effective in releasing the free amino acids from peptides. Of these amino acids, the concentrations of arginine, lysine, histidine, tyrosine, phenylalanine, leucine, and glutamine were increased much more than those of other amino acids. This indicated that both the porcine pancreatic exopeptidases preparation and the IPPE contained carboxypeptidase A, B, and aminopeptidase. The IPPE was also efficient in the decrease of the hydrophobicity of protein hydrolysates demonstrated by hydrophobic chromatographic analysis. This led to the application of the immobilized exopeptidases in protein hydrolysate debittering. The IPPE was able to remove the bitterness of the tryptic/chymotryptic casein hydrolysates.
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PMID:The immobilized porcine pancreatic exopeptidases and its application in casein hydrolysates debittering. 867 84

The objective of this research was to formulate a mixture of commercial proteases that would mimic the rate and extent of protein degradation obtained using strained ruminal fluid. The proteolytic activity of strained ruminal fluid and several commercial proteases was characterized using 13 L-amino acid p-nitroanilides as artificial substrates. A mixture of Streptomyces griseus protease, chymotrypsin, and proteinase K at .042, 2.5, and .5 enzyme units/mL, respectively, was similar to the activity of strained ruminal fluid against the same artificial substrates. However, degradative activities were different in incubations with feed proteins as substrates. The rates of degradation of expeller soybean meal, solvent soybean meal, and casein were .08, .05, and .08/h, respectively, using the enzyme mixture and .03, .15, and .24/h using strained ruminal fluid. A second experiment compared degradative activity of S. griseus protease at .066 enzyme units/mL, ficin at .5 enzyme units/mL, and a mixture of trypsin, carboxypeptidase B, chymotrypsin, and carboxypeptidase A at 116.6, .5, 2.5, and .5 enzyme units/mL, respectively. Protein degradation rates obtained with strained ruminal fluid were two to six times faster than those obtained with the enzyme mixtures. A third experiment compared the degradability of 15 feed proteins with the mixture of trypsin, carboxypeptidase B, chymotrypsin and carboxypeptidase A to that with strained ruminal fluid. Degradation rates obtained using strained ruminal fluid ranged from .007 to .217/h; degradation rates using the enzyme mixture ranged from .010 to .079/h and were lower (P = .004) than with strained ruminal fluid. Overall, the experiments indicated that the commercial enzymes tested did not mimic the protein degradative activity of strained ruminal fluid.
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PMID:Characterization of the proteolytic activity of commercial proteases and strained ruminal fluid. 870 28


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