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)

Effects of proteinase inhibitors on total proteolytic activity and trypsin and chymotrypsin activity in human pancreatic juice were determined separately. Purified inhibitors as well as crude extracts of raw soybeans completely inhibited trypsin and chymotrypsin activity while 40 to 50% of the total proteolytic activity remained. Inhibition experiments with 1,10-o-phenanthroline showed that this residual proteolytic activity was due mainly to carboxypeptidase A and B. Comparative studies with rat pancreatic enzymes demonstrated certain similarities between the corresponding enzymes from rat and man. However, differences were revealed which indicate that the rat enzymes must be used with great caution when applied as models for the human proteinases when studying effects of soybean inhibitors.
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PMID:Inhibition of human and rat pancreatic proteinases by crude and purified soybean proteinase inhibitors. 57 Oct 12

The interaction of human plasma alpha-1-antichymotrypsin with serine proteinases from different tissues has been investigated. The protein was found to form stable complexes with pancreatic chymotrypsin, leukocyte cathepsin G, and mast cell chymotrypsin. No inhibition of pancreatic trypsin or leukocyte elastase could be demonstrated. With mixtures containing both alpha-1-antichymotrypsin and alpha-1-proteinase inhibitor, it was found that the former preferentially inactivated leukocyte cathepsin G, while the latter showed a strong preference for pancreatic chymotrypsin. However, leukocyte elastase was specifically inactivated by alpha-1-proteinase inhibitor even in 1:1 mixtures with chymotrypsin. All of these results taken together suggest that one of the primary functions of alpha-1-antichymotrypsin is to inactivate leukocyte cathepsin G, while alpha-1-proteinase inhibitor controls the activity of other serine proteinases, particularly leukocyte elastase.
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PMID:Human alpha-1-antichymotrypsin: interaction with chymotrypsin-like proteinases. 72 23

Nitration of bovine carboxypeptidase A crystals with tetranitromethane increases esterase activity, decreases peptidase activity, and modifies about one tyrosyl residue. Modification of enzyme crystals avoids the polymerization that occurs when the enzyme is nitrated in solution. Two procedures have been employed to identify the tyrosyl residues nitrated. The first involves cyanogen bromide cleavage and isolation of the fragment containing residues 104-301. After solubilization by succinylation, this fragment is digested with chymotrypsin, the peptides are fractionated by gel filtration, and the nitrotyrosyl peptides are purified by affinity chromatography on an antinitrotyrosyl antibody-Sepharose conjugate followed by ion-exchange chromatography. In the second, the nitroenzyme is heat denatured, digested by chymotrypsin, and fractionated on the affinity and ion-exchange columns. By both methods, the major mitropeptides, representing between 60 and 80% of the nitrotyrosyl label, are uniquely compatible with that segment of the sequence of carboxypeptidase containing Tyr-248. A nearby cation, either the active site zinc ion or Arg-145, would seem to be an important factor in determining the selective nitration of this residue.
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PMID:Chemical modification of carboxypeptidase A crystals. Nitration of tyrosine-248. 94 53

The seminal plasma and sperm of fresh and stored poultry semen were analyzed for the presence of eight peptide hydrolase enzymes. Five enzymes: carboxypeptidase A, carboxypeptidase B, chymotrypsin, glycylglycylglycine hydrolase and pepsin were not present in either plasma or sperm. An aminopeptidase-like and a cathepsin-like activity were found in seminal plasma and sperm while a trypsin-like activity was found in sperm only. There was a significant difference between full sib groups with respect to aminopeptidase-like activity in fresh and stored plasma, while storage for 24 hours resulted in a significant increase in trypsin-like activity of sperm. The aminopeptidase-like activity of fresh sperm was positively correlated with duration and percent fertility of fresh semen, while neither cathepsin-like activity nor trypsin-like activity were correlated with fertility of fresh or stored semen except for a positive correlation between the cathepsin-like activity of fresh plasma and percent fertility of fresh semen.
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PMID:The activity of some peptide hydrolase enzymes in fresh and stored poultry semen from full sib groups of males and their relationship to fertility. 118 12

Axon reflex vasodilation following injury to the skin of the pinna of the ear was studied in rats by a thermometric method. Post-traumatic vaso-dilatation did not occur in animals treated with tyrosine ethyl ester, an inhibitor of chymotrypsin. Vasodilatation was not affected by treatment of the rats with chlorpheniramine (antihistamine) or cyproheptadine (antihistamine and anti-serotinin) or with aprotinin, soybean trypsin inhibitor, epsilon-aminocaproic acid or tosyl arginine methyl ester (inhibitors of trypsin and of some other proteinases). Taken in conjunction with the results of other investigations, these findings indicate that in the skin of the rat: (a) histamine and serotinin are not essential for the initiation of axon reflexes, and (b) the chymotrypsin-like proteinase of mast cell granules, released as the result of antidromic activity in sensory axons, may act as a kininogenase and be responsible for causing dilatation of arterioles at the efferent limb of the axon reflex.
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PMID:Evidence for the involvement of vasoactive constitutents of mast cells in axon reflex vasodilatation in the skin of the rat. 125 6

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 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

Changes in the activities of three gastric and nine pancreatic enzymes plus colipase were determined during postnatal development and weaning in calves. In calves exclusively milk-fed for 2, 7, 28, 56, 70 and 119 d, the enzyme activities per kilogram of empty live weight increased with age for chymotrypsin, elastase, carboxypeptidases A and B, ribonuclease and alpha-amylase, decreased for chymosin, lysozyme and colipase but showed no change in the case of pepsin, trypsin, lipase and phospholipase A2 compared with animals at birth. The greatest increase was that in alpha-amylase activity (about 50-fold between d 2 and 119). In calves weaned between d 28 and 56, all the activities were higher than in milk-fed animals, except that of chymosin (which was slightly lower) and that of colipase (which did not change). At 119 d of age, chymotrypsin, carboxypeptidase A, alpha-amylase and lipase were 1.6- to fourfold higher in ruminants than in preruminants. Thus, most enzyme activities were modified first by colostrum and milk intake, and again upon weaning by development of the forestomachs and ingestion of solid food. These ontogenic patterns might be under the control of many gut regulatory peptides, the plasma concentrations of which changed simultaneously. Some gastric and pancreatic enzymes were correlated to plasma concentrations of these gut regulatory peptides.
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PMID:Gastric and pancreatic enzyme activities and their relationship with some gut regulatory peptides during postnatal development and weaning in calves. 137 46

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

Reinvestigation of the structure of the beta-chain of Hb Atlanta-Coventry (beta 75 Leu----Pro, beta 141 Leu deleted) confirmed the presence of two abnormalities; however, analysis of the aberrant beta Co14 tryptic peptide by liquid secondary ion mass spectrometry indicated that the beta 141 Leu (mass 113 daltons) was not deleted but replaced by a novel amino acid of mass 129 daltons. The new amino acid in peptide beta Co14 was uncharged at pH 6.5, more hydrophillic than leucine and susceptible to cleavage by both chymotrypsin and carboxypeptidase A. We propose that the new residue is likely to be hydroxyleucine and that it results from post-translational oxidation of beta 141 Leu as a consequence of perturbation of the haem environment caused by the beta 75 Leu----Pro mutation in the E helix (E19). This proposal is entirely consistent with recent DNA analysis which showed that beta At-Co was not the product of a third beta-globin gene and that neither of the two beta-globin genes, beta A nor beta Atlanta, contained a deletion of the beta 141 Leu codon. We have subsequently found this modified amino acid at position beta 141 in two other unstable haemoglobins, both of which involve mutations on the haem side of the E helix.
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PMID:Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-Coventry but is replaced by a novel amino acid of mass 129 daltons. 152 Jun 32


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