Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.27.4 (ribonuclease)
6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Treatment of spectrin, insulin, glucagon and ribonuclease with ozone results in covalent cross-linking of these proteins. This cross-linking is not reversed by treatment with dithiothreitol and thus can not be ascribed to -S-S- bond formation. A concomitant O,O'-dityrosine formation is observed by spectrofluorometric analysis of the protein and by amino acid analysis and thin-layer chromatography of hydrolyzed protein samples. It is highly probable that the observed protein cross-linking should be attributed to interpeptide O,O'-dityrosine bonds. Several authors have shown before that oxidation of proteins with horseradish peroxidase and H2O2 also leads to O,O'-dityrosine formation. Peroxidase-induced O,O'-dityrosine formation in galactose oxidase (d-galactose:oxygen 6-oxidoreductase, EC 1.1.3.9) causes a strong increase of enzyme activity. In accordance with these observations ozone treatment of galactose oxidase also leads to O,O'-dityrosine formation with a concomitant 8-fold increase of enzyme activity.
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PMID:Ozone-induced formation of O,O'-dityrosine cross-linked in proteins. 704 79

A novel, rapid and simple method for the preparation of emulsion-templated monoliths in microfluidic channels based on thiol-ene chemistry is presented. The method allows monolith synthesis and anchoring inside thiol-ene microchannels in a single photoinitiated step. Characterization by scanning electron microscopy showed that the methanol-based emulsion templating process resulted in a network of highly interconnected and regular thiol-ene beads anchored solidly inside thiol-ene microchannels. Surface area measurements indicate that the monoliths are macroporous, with no or little micro- or mesopores. As a demonstration, galactose oxidase and peptide-N-glycosidase F (PNGase F) were immobilized at the surface of the synthesized thiol-ene monoliths via two different mechanisms. First, cysteine groups on the protein surface were used for reversible covalent linkage to free thiol functional groups on the monoliths. Second, covalent linkage was achieved via free primary amino groups on the protein surface by means of thiol-ene click chemistry and l-ascorbic acid linkage. Thus prepared galactose oxidase and PNGase F microreactors demonstrated good enzymatic activity in a galactose assay and the deglycosilation of ribonuclease B, respectively.
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PMID:Rapid and simple preparation of thiol-ene emulsion-templated monoliths and their application as enzymatic microreactors. 2585 Sep 55