Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

Comparative differences between tibial dyschondroplastic (TD) and age-matched control turkey epiphyseal cartilages were studied using cellular, metabolic, and extracellular matrix characteristics. Alkaline phosphatase and aryl sulfatase activities were measured as variables of calcification and cartilage degradation, respectively. There was a decrease in the activities of both enzymes in TD tissues. An increase in tissue phosphate concentrations was noted in the TD tissue whereas neither tissue calcium nor serum calcium and phosphorous concentrations were affected. Profiles of noncollagenous and collagenous proteins from normal and TD-affected tissues were compared following in vitro biotinylation of epiphyseal cartilage followed by a sequential extraction using 4 M guanidine HCl and pepsin digestion, respectively. Electrophoretically separated proteins from both extracts were analyzed on Western blots and compared for any prominent differences between normal and TD cartilages. Biotinylation enhanced the detectability of extracted proteins. There were, however, no major differences in the patterns of noncollagenous or collagenous proteins between the two groups of tissues. Tibial dyschondroplastic lesions further exhibited a large number of dead chondrocytes, which increased with severity of lesion. There appears to be no significant difference in the pattern of extracellular-matrix-associated proteins. However, enzyme and metabolic activities of TD-affected cartilages were significantly reduced, and this may be due to premature death of chondrocytes in the process of development.
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PMID:Physiological studies of turkey tibial dyschondroplasia. 817 20

Automated analyses were used to determine the effect of retinol on the activity of the following proteolytic enzymes: ficin (EC 3.4.4.12), bromelain (EC 3.4.4. 24), trypsin (EC 3.4.4.4.), chymotrypsin A (EC 3.4.4.5), papain (EC 3.4.4.10), clostridiopeptidase A (EC 3.4.4.19), pepsin (EC 3.4.4.1), cathepsin D (EC 3.4.4. 23) from rat-liver and rat-kidney lysosomes and the nonspecific proteolytic enzyme, pronase. Of these proteolytic enzymes only ficin, bromelain, and rat-kidney lysosomal cathepsin D were inhibited significantly by 1x10(-4) M retinol.Some nonproteolytic enzymes not inhibited by retinol were acid phosphatase (EC 3.1.3.2), beta-acetylglucosaminidase (EC 3.2.1.30), arylsulfatase (EC 3.1.6.1), and pyruvate kinase (EC 2.7.1.40). The inhibition of cathepsin D varied with the substrate used, being greater with hemoglobin than with ovalbumin or bovine serum albumin. Carotene and retinol inhibited ficin and cathepsin D to similar extents. Retinol inhibition of ficin was partially reversible. These studies of proteolytic enzyme inhibition by retinol serve as a simple model for studying retinol-protein interactions in vitro.
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PMID:Retinol inhibition of some proteolytic enzymes. 1780 59

Cystine knots or nested disulfides are structurally difficult to characterize, despite current technological advances in peptide mapping with high-resolution liquid chromatography coupled with mass spectrometry (LC-MS). In the case of recombinant human arylsulfatase A (rhASA), there is one cystine knot at the C-terminal, a pair of nested disulfides at the middle, and two out of three unpaired cysteines in the N-terminal region. The statuses of these cysteines are critical structure attributes for rhASA function and stability that requires precise examination. We used a unique approach to determine the status and linkage of each cysteine in rhASA, which was comprised of multi-enzyme digestion strategies (from Lys-C, trypsin, Asp-N, pepsin, and PNGase F) and multi-fragmentation methods in mass spectrometry using electron transfer dissociation (ETD), collision induced dissociation (CID), and CID with MS(3) (after ETD). In addition to generating desired lengths of enzymatic peptides for effective fragmentation, the digestion pH was optimized to minimize the disulfide scrambling. The disulfide linkages, including the cystine knot and a pair of nested cysteines, unpaired cysteines, and the post-translational modification of a cysteine to formylglycine, were all determined. In the assignment, the disulfide linkages were Cys138-Cys154, Cys143-Cys150, Cys282-Cys396, Cys470-Cys482, Cys471-Cys484, and Cys475-Cys481. For the unpaired cysteines, Cys20 and Cys276 were free cysteines, and Cys51 was largely converted to formylglycine (>70%). A successful methodology has been developed, which can be routinely used to determine these difficult-to-resolve disulfide linkages, ensuring drug function and stability.
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PMID:Complete mapping of a cystine knot and nested disulfides of recombinant human arylsulfatase A by multi-enzyme digestion and LC-MS analysis using CID and ETD. 2320 45