Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The combined use in peptide synthesis of the Fmoc-group with methyl, benzyl or p-nitro benzyl esters is not practical because of the elimination of the Fmoc-group under basic conditions and by catalytic hydrogenation. Nevertheless the solution synthesis of peptides requires those combinations in some cases. For this purpose we have investigated enzymatic hydrolysis of some tri and tetrapeptide esters. The hydrolysis were carried out under pH-control. We measured deprotection of the carboxyl group by thermitase, porcine liver esterase, carboxypeptidase A and alpha-chymotrypsin. The main problems are to suppress proteolytic degradation of the peptide bond and to bring the protected peptides into solution. To solve both problems we used dimethylformamide and dimethylsulfoxide as cosolvents. The ratios between esterolytic and proteolytic activity were estimated under various cosolvent concentrations. Advantages of this method are to avoid side reactions of alkaline instable side chains (e.g. asparagine, glutamine), cleavage of base labile protecting groups and racemization by alkaline saponification. The enzymatic deprotection was followed by HPLC, HPTLC and titration. On a preparative scale this method gives good yields and sufficiently pure products.
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PMID:Hydrolysis of peptide esters by different enzymes. 144 67

In the study of the covalent immobilization of aminoacylase, thermitase, pepsin, trypsin, chymotrypsin, elastase, subtilisin, penicillinamidohydrolase, carboxypeptidase A, cystathionine-beta-synthase, and anticathepsin D-IgG to copolymers of 2-hydroxyethyl methacrylate and ethylene dimethacrylate (Separon HEMA) containing epoxy groups a marked influence of added salts on the immobilization efficiency was observed. Yields in covalently bound active enzymes were dependent on the concentrations and type of ions added, which can be arranged according to the Hofmeister series. At a distinct concentration, the salting-out ions cause a protein-matrix hydrophobic interaction which is a prerequisite for the covalent bond formation.
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PMID:Influence of salts on the covalent immobilization of proteins to modified copolymers of 2-hydroxyethyl methacrylate with ethylene dimethacrylate. 340 61