Coefficiente di estinzione: E1% = 21,0 (280 nm) pI: 9,0
Azioni biochim/fisiol
La ficina è classificata come proteasi tiolica. Contiene una singola cisteina reattiva nel sito attivo. L′omologia degli amminoacidi del sito attivo è simile a quella della papaina. La ficina scinde le proteine in corrispondenza del lato carbossilico di Gly, Ser, Thr, Met, Lys, Arg, Tyr, Ala, Asn e Val. La Km del substrato cromogenico pGlu-Phe-Leu-p-nitroanilina è di 0,43 mM. La ficina è inibita da: iodoacetamide, acido iodoacetico, N-etilmaleimide, cloruro mercurico, DFP (diisopropil fluorofosfato), TLCK (Na-p-Tosil-lisina clorometil chetone) e TPCK (N-Tosil-L-fenilalanina clorometil chetone). La ficina può essere utilizzata per generare frammenti F (ab′)2 ad alta resa a partire dalla IgG1 di topo.
Definizione di unità
L′enzima è solubile in 1 M di tampone di fosfato di potassio, pH 7,0 (0,25 mg/ml), e produce una soluzione trasparente.
Un′unità produce un ΔA280 di 1,0 per minuto a pH 7,0 e 37 °C, misurato come prodotti solubili in TCA dalla caseina in un volume finale di 10 ml (percorso luminoso di 1 cm).
Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for
Journal of immunological methods, 312(1-2), 167-181 (2006-05-06)
The sensitivity of immunosensors is strongly dependent on the amount of immobilised antibodies and their remaining antigen binding properties. The use of smaller and well-oriented antibody fragments as bioreceptor molecules influences the final immunosensor signal. The aim of this study
The capability of ficin, a cystine protease, to form peptide bonds was investigated using several types of N-Boc-amino acid phenyl and naphthyl esters as acyl donor components. Enzyme-catalyzed peptide synthesis was carried out under optimized reaction conditions of pH, acyl
Molecular cancer therapeutics, 7(1), 143-151 (2008-01-19)
2-[(1-methylpropyl)dithio]-1H-imidazole (IV-2) is a known inhibitor of the thioredoxin system. It causes the oxidation of cysteine residues from both thioredoxin reductase and thioredoxin, with only the latter leading to irreversible inhibition of protein function. Although IV-2 is considered to be
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 141(1), 103-109 (2005-04-12)
A novel cysteine protease inhibitor (Eel-CPI-1) was isolated from the epidermis of the eel. Eel-CPI-1 was shown to bind strongly to both lactose- and carboxymethylated papain-affinity gels. Its molecular mass under reducing condition was determined to be 18 kDa by
This procedure may be used for all Ficin products.
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