1,721,047 research outputs found
Processo per ottenere un rivestimento neoceramico di protesi metalliche per osseointegrazione
No full textTitanium Carbide Coatings to be applied on osteintegrative prosthesis in biomedical applications
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Caratterizzazione con tecniche tradizionali ed innovative di rivestimenti in carburo di titanio per applicazione biomedicale
No full textProcesso per ottenere un rivestimento neoceramico di protesi metalliche per osseointegrazione
No full textFUNCTIONAL RESIDUES AT THE ACTIVE SITE OF HORSE LIVER PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE.
No full textHorse liver phosphopantothenoylcysteine decarboxylase (EC 4.1.1.36) is rapidly inactivated by N-acetoacetylation with diketene following a pseudo-first-order kinetics: the presence of substrate quantitatively protects against this inactivation. Histidine photo-oxidation with methylene blue or rose bengal brings about the total loss of activity. These results indicate the presence of functional lysyl and histidyl groups at the active site of the enzyme. The substrate sulphydryl group is essential for enzyme activity. Enzymatic decarboxylation is proposed to result from a combined action of the keto group of the enzyme-bound pyruvate protonated by an essential histidine and a protonated amino group of a lysine
Effect of pH salt and temperature on the association of recombinant wt amidase from Sulfolobus solfataricus and on its mutant Y41C.
No full textMolecular and biochemical characterization of the recombinant amidase from hyperthermophilic archaeon Sulfolobus solfataricus
No full textWe have cloned, sequenced, and overexpressed in Escherichia coli the amidase gene from the hyperthermophilic archaeon Sulfolobus solfataricus (strain MT4). The recombinant thermophilic protein was expressed as a fusion protein with an N-terminus six-histidine-residue affinity tag. The enzyme, the first characterized archaeal amidase, is a monomer of 55,784 daltons, enantioselective, and active on 2- to 6-carbon aliphatic amides and on many aromatic amides, over the pH range 4-9 and at temperatures from 60 degrees to 95 degreesC. The S. solfataricus amidase belongs to the class of amidases that share a characteristic signature, GGSS(S/G)GS, located in the central region of the protein, and which show remarkable variability in their individual substrate specificities, can hydrolyze aliphatic or aromatic substrates, and share a large invariance of their primary structure
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