Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.1.6.1 (sulfatase)
3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A technique utilizing Pregnant Mare's Serum Gonadotropin and Human Chorionic Gonadotropin treatment of hens (Gallus domesticus), followed by manual ovulation of the excised follicles, was developed to obtain a large number of mature ova. The intact ova were used to test whether acrosin, partially purified from the spermatozoa of the cock (Gallus domesticus), partially purified rabbit testicular acrosin and commercial preparations of several hydrolytic enzymes could dissolve the inner vitelline membrane. Enzymes were applied to pieces of filter paper placed on the ovum. Cock acrosin and endopeptidases such as trypsin, chymotrypsin, collagenase and elastase hydrolyzed the membrane whereas exopeptidases such as leucine aminopeptidase and carboxypeptidase A did not. Phospholipase A, sulfatase, hyaluronidase, beta-glucuronidase and rabbit testicular acrosin also failed to hydrolyze the membrane. Cock acrosin hydrolysis of the ovum surface was inhibited by soybean trypsin inhibitor. The surface of the ovum over the germinal disc region was hydrolyzed more quickly by cock acrosin than the surface over other regions of the ovum. Acrosin from cock sperm caused the release of trichloroacetic acid soluble material absorbing at 280 nm from sonicated preparations of inner vitelline membranes. Hydrolysis was greatest at pH 8.0 and was inhibited by soybean trypsin inhibitor.
...
PMID:Hydrolysis of the hen egg vitelline membrane by cock sperm acrosin and other enzymes. 0 Apr 54

The availability of a patient with basophilic leukemia manifesting 75 to 90% mature basophils permitted the use of a cell concentration sufficient to generate and release mediators upon interaction with a calcium ionophore in quantities adequate for their physiocochemical characterization. The mediators were defined in terms of their physicochemical characteristics: slow reacting substance of anaphylaxis (SRS-A) by purification through silicic acid chromatography and inactivation by arylsulfatase; eosinophil chemotactic factor of anaphylaxis (ECF-A) by its gel filtration through Sephadex G-25 and inactivation by subtilisin and not trypsin; and platelet-activating factor (PAF) by its inherent binding to albumin. Both ECF-A and histamine were present in their preformed state, and for histamine it was possible to establish that the concentration per cell was comparable to that of normal human basophils. Dibutyryl cyclic AMP suppressed release of histamine and SRS-A, indicating that their availability was under a control similar to that observed with normal cells subjected to immunologic activation. The demonstration that a suspension of leukemic human basophils contained the preformed mediators, histamine and ECF-A, and generated SRS-A and PAF for release along with histamine and ECF-A, after activation with a calcium ionophore, establishes that a single cell type can serve as a source of the four recognized mediators of immediate-type hypersensitivity.
...
PMID:The release of four mediators of immediate hypersensitivity from human leukemic basophils. 4 47

Investigation of pure human pancreatic juice obtained by direct cannulation of the main pancreatic duct of 11 healthy volunteer subjects and 10 chronic alcoholics without detectable pancreatic disease revealed the presence of numerous acid hydrolases in this secretion. The pH optimal and substrate specificities of these enzymes suggest that they are of lysosomal origin. Stimulation of the pancreas by injection of cholecystokinin-pancreozymin (CCK-PZ) (1 Ivy dog unit/kg) resulted in a striking increase in activity of some of these hydrolases (N-acetyl-beta-D-glucosaminidase, arylsulfatase, etc.) similar to that observed for trypsin, amylase, and other pancreatic digestive enzymes. In a second group of hydrolases (beta-D-glucuronidase, leucine naphthylamidase, etc.) the effect of this hormone was greatly reduced or absent, particularly in normal individuals. In chronic alcoholics enzyme activity in response to CCK-PZ injection was greater than in normal subjects. Although this increase achieved statistical significance (P less than 0.05) in the case of beta-D-glucuronidase only, it was observed for all lysosomal hydrolases tested and suggests either increased synthesis or a more facile release of these enzymes from the pancreas of chronic alcoholics than of normal individuals.
...
PMID:Lysosomal enzymes in pure pancreatic juice from normal healthy volunteers and chronic alcoholics. 45 5

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
...
PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

Chronic exposure of rats to 10% aerosols of papain or trypsin resulted in marked increases in lung weights and lung beta-glucuronidase and arylsulfatase activities. Destruction of alveolar walls was demonstrated microscopically as a decrease in the number of air spaces touching a line of known length. The pregnenes, progesterone and medroxyprogesterone acetate, but not the 19-nortestosterone derivative norethindrone, partially prevented the papain-induced breakdown of alveolar septa and elevation of beta-glucuronidase. The steroidal anti-inflammatory agent, paramethasone, completely inhibited the rise in lung weight and beta-glucuronidase activity, but did not prevent destruction of alveolar walls. The non-steroidal anti-inflammatory agent, indomethacin, afforded little or no protection. Limited prophylaxis against both histological and enzymatic changes was observed in rats treated with the anti-metabolite, cyclophosphamide, and the proteolytic enzyme inhibitor, aprotinin. The various lung abnormalities resulting from papain inhalation may thus be individually influenced by specific pharmacologic agents.
...
PMID:Lung enzymes in emphysematous rats: effects of progestagens, antiphlogistics and metabolic inhibitors. 116 8

Arylsulfatase A purified from human placenta contained an unreported component with an apparent molecular mass of 7 kDa in addition to the two known components with apparent molecular masses of 58 and 50 kDa. The detailed relationship between the 58 kDa component and the 50 kDa component is as yet unknown. The present study was undertaken to define the structure of the subunits of the sulfatase. The N-terminal sequence of the 50 kDa component was identical to that of the 58 kDa component. Furthermore, the peptide maps of the 50 kDa component, which was separately digested with trypsin and Achromobacter proteinase I, were quite similar to those of the 58 kDa one. Through sequence analysis of the incompatible peaks in the peptide maps, the 50 kDa component was found to lack a sequence from Val-445 to the C-terminus. On the other hand, the N-terminal sequence of the 7 kDa component began with Ala-448, though there was a minor sequence commencing with Thr-449. These observations suggest that the 50 and 7 kDa components were produced by limited proteolysis near the C-terminus of the 58 kDa component. Through analysis using unreducing SDS-PAGE, the 58 and the 7 kDa components were found to be linked by disulphide bonds. Arylsulfatase A purified from human liver was also composed of the same subunits as the placental one. This finding suggests that human arylsulfatase A undergoes similar proteolytic processing regardless of the tissue involved.
...
PMID:Proteolytic processing of human lysosomal arylsulfatase A. 135 93

The processing of preprocholecystokinin in human pituitary extracts was investigated using gel and ion-exchange chromatography monitored by sequence-specific radioimmunoassays before and after incubation with trypsin, carboxypeptidase B, and arylsulfatase. Whereas the neural lobe contained only the bioactive alpha-carboxyamidated cholecystokinin (CCK) peptides (32 pmol/g), of which CCK-8 predominated, the anterior lobe contained substantial amounts of three large nonamidated procholecystokinin fragments (95 pmol/g; Mrs, 9000, 7000, and 5000) and small amounts of alpha-amidated CCK (8.3 pmol/g). The latter occurred only in the following large molecular forms: component I, CCK-58, and traces of CCK-33. Corticotrophic tumors processed the large forms to small CCK-8-like forms as are found in the brain and in the gut. The results show that a hormone gene, although translated, is expressed only to a limited extent as mature, active peptide outside the principal production region(s). Thus the processing of CCK to small alpha-amidated peptides in the less-differentiated tumor tissue supports the hypothesis that differentiation of endocrine cells may be sustained also at the posttranslational level.
...
PMID:Preprocholecystokinin processing in the normal human anterior pituitary. 347 48

Using gel, ion-exchange, and reverse-phase chromatography monitored by radioimmunoassays specific for five sequences of preprocholecystokinin (prepro-CCK), its processing products were measured in neutral and acid extracts of porcine cerebral cortex before and after incubation with trypsin, carboxypeptidase B, and arylsulfatase. Three categories of peptides were found: biologically active peptides, i.e. peptides with the alpha-amidated COOH terminus Trp-Met-Asp-Phe-NH2, comprising large CCKs, i.e. peptides larger than CCK-58 and peptides eluting like CCK-58, CCK-33, and CCK-22; CCK-octapeptides in sulfated and traces of nonsulfated forms; and small CCKs, i.e. traces of CCK-7, large amounts of CCK-5, and modest concentrations of CCK-4 (the structures of CCK-5 and -4 were confirmed by sequence analysis); four NH2-terminal fragments, of which the two predominant ones correspond to the desnonapeptide fragments of CCK-58 and CCK-33; and COOH-terminal extended peptides corresponding to glycine-extended CCK-58, CCK-33, and CCK-8 in small but significant amounts. Thus, in addition to CCK-8 the porcine cerebral cortex synthesizes larger and smaller active CCK peptides in quantities of an order similar to those of CCK-8. The occurrence of these together with the NH2-terminal fragments and glycine-extended peptides can be explained only by the existence of different processing pathways for preproCCK. Consequently, the results suggest that cerebral CCK neurons are heterogeneous and comprise at least three populations with different biosynthetic machineries.
...
PMID:Characterization of preprocholecystokinin products in the porcine cerebral cortex. Evidence of different processing pathways. 370 Mar 74

Using gel and ion-exchange chromatography monitored by radioimmunoassays specific for sequences essential in the processing of preprogastrin and preprocholecystokinin, the products were characterized in extracts of porcine pituitary lobes before and after incubation with trypsin, carboxypeptidase B, and arylsulfatase. The intermediate and neural lobes contained only fully activated (i.e. alpha-amidated) preprogastrin products (component I, gastrin-34, and gastrin-17). In contrast, the anterior lobe contained, in addition to traces of alpha-amidated gastrin (2 pmol/g), hundredfold higher amounts of a nonamidated progastrin (189 pmol/g; Mr approximately 7000) and two nonamidated procholecystokinin fragments (75 pmol/g; Mr approximately 7000 and 5000). These results show that hormone genes, in spite of translation of their mRNA, are not necessarily expressed in functional peptides in cells outside the principal production regions. Hence, the study indicates that differentiation of endocrine cells may be controlled at the post-translational level.
...
PMID:Accumulation of nonamidated preprogastrin and preprocholecystokinin products in porcine pituitary corticotrophs. Evidence of post-translational control of cell differentiation. 370 Mar 75

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
...
PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42


1 2 3 Next >>

---