Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The use of caprylate for the inactivation of lipid-enveloped viruses in biologically active proteins both plasma derived and produced by cell culture was evaluated. Viruses consisted of herpes simplex virus type I, vesicular stomatitis virus, vaccinia virus, and Sindbis virus. Utilizing the dissociation reaction and varying the concentration of the ionized form of caprylate, a specific amount of the nonionized form of caprylate was maintained over a wide pH range. Virus-spiked protein solutions contacted with caprylate provide rapid virus inactivation under a variety of conditions while maintaining the integrity of the respective protein or activity. With the exception of coagulation factor AHF, protein and biological activity yield were essentially quantitative. Caprylate is removed after treatment by size exclusion chromatography or anion/cation exchange adsorption of the protein, followed by buffer wash.
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PMID:Inactivation of lipid-enveloped viruses in proteins by caprylate. 203 41

In an effort to facilitate studies of the reaction involved in the removal of fatty acids from acyl proteins, we have synthesized an octanoic acid ester of doubly blocked serine, specifically octanoyl N-carbobenzoxy-L-serine-benzyl ester (octanoyl boc-serine), and used it as a substrate to guide the purification of an esterase from rat lung. The esterase was purified 228-fold by column chromatography on DE-52 cellulose, hydroxylapatite, octyl-Sepharose, and concanavalin A-Sepharose and by HPLC gel filtration. The final enzyme preparation ran as a single 77,000-Da band when subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and exhibited a single symmetrical peak (sedimentation coefficient, 4.5 S) when centrifuged through a sucrose density gradient (empirical Mr, 63,000). The esterase is an acidic protein, pI 4.1, and is very active against p-nitrophenyl esters comprised of C4-C14 fatty acids; the highest specific activity (26.5 mumol/min/mg) was obtained using p-nitrophenyl caprylate as substrate. The pH optimum of the lung esterase is near 8.0 and the activity on octanoyl boc-serine is maximum when 0.3% (w/v) Myrj-52 is included in the assay medium. The activity of the esterase is not dependent on calcium ions. The enzyme does not remove acyl groups from the G-protein of vesicular stomatitis virus or the proteolipid of bovine brain. The possible role of the esterase in the metabolism of acylated proteins is considered.
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PMID:Isolation and characterization of a fatty acyl esterase from rat lung. 335 57