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)

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

Here the structure of human glyoxalase II has been investigated by studying unfolding at equilibrium and refolding. Human glyoxalase II contains two tryptophan residues situated at the N-terminal (Trp57) and C-terminal (Trp199) regions of the molecule. Trp57 is a non-conserved residue located within a "zinc binding motif" (T/SHXHX57DH) which is strictly conserved in all known glyoxalase II sequences as well as in metal-dependent beta-lactamase and arylsulfatase. Site-directed mutagenesis has been used to construct single-tryptophan mutants in order to characterize better the guanidine-induced unfolding intermediates. The denaturation at equilibrium of wild-type glyoxalase II, as followed by activity, intrinsic fluorescence and CD, is multiphasic, suggesting that different regions of varying structural stability characterize the native structure of glyoxalase II. At intermediate denaturant concentration (1.2 M guanidine) a molten globule state is attained. The reactivation of the denatured wild-type enzyme occurs only in the presence of Zn(II) ions. The results show that Zn(II) is essential for the maintenance of the native structure of glyoxalase II and that its binding to the apoenzyme occurs during an essential step of refolding. The comparison of unfolding fluorescence transitions of single-trypthophan mutants with that of wild-type enzyme indicates that the strictly conserved "zinc binding motif" is located in a flexible region of the active site in which Zn(II) participates in catalysis.
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PMID:Unfolding and refolding of human glyoxalase II and its single-tryptophan mutants. 1043 33

Hydrogen-deuterium exchange can be a sensitive indicator of protein structural integrity. Comparisons were made between cerebroside sulfate activator protein (CSAct) in the native state and after treatment with guanidine hydrochloride plus dithiothreitol. Native protein has three internal disulfide bonds and treated protein has no internal disulfide bonds. The comparisons were made using hydrogen-deuterium exchange measured by electrospray ionization mass spectrometry, percentage alpha-helical content measured by circular dichroism and biological activity measured by the ability to support arylsulfatase A-catalyzed sulfate hydrolysis from cerebroside sulfate. In acidic solvent native protein has 59 exchange refractory protons and treated protein has 20 exchange refractory protons (44 and 14% of the exchangeable proton populations, respectively). In native protein the size of the exchange refractory proton population is sensitive to changes in pH, temperature and the presence of a ligand. It is uninfluenced by the presence or absence of glycosyl groups attached to Asn21. Helical content is virtually identical in native and treated protein. Biological activity is significantly reduced but not obliterated in treated protein. The hydrogen-deuterium exchange profile appears to be a sensitive signature of the correctly folded protein, and reflects a dimension of the protein structure that is not apparent in circular dichroic spectra or in the ability of the protein to support arylsulfatase A-catalyzed sulfate hydrolysis from sulfatide. The hydrogen-deuterium exchange profile will be a valuable criterion for characterizing mutant forms of CSAct produced by recombinant and synthetic paradigms and also the native and mutant forms of related proteins.
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PMID:Hydrogen-deuterium exchange signature of porcine cerebroside sulfate activator protein. 1076 69