A mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid.
Specificità
Una miscela di almeno tre attività proteolitiche inclusa una serin proteasi extracellulare. In generale, le serin proteasi mostrano un′ampia gamma di specificità per il substrato, che si ritiene siano mediate da un sito attivo composto da un residuo Asp, un residuo His e un residuo Ser nella molecola. Questo enzima preferisce idrolizzare i legami peptidici sul lato carbossilico dell′acido glutammico o aspartico.
Applicazioni
La proteasi è usata di solito nelle procedure di isolamento degli acidi nucleici in incubazioni di 0,5-3,0 ore con aggiunta di sodio dodecil solfato 0,2% ed EDTA 10 mM.
Questo enzima è più attivo in un intervallo di pH più alto rispetto alla proteasi alcalina nota, mostrando l′attività proteolitica perfino in una soluzione 0,2 N di NaOH. Questo enzima è utile per la proteolisi di proteine insolubili e per lo studio della struttura delle proteine.
Suitable for:
Nucleic acid isolation procedures in incubations
Degrade protein during nucleic acid purification
Proteolysis of insoluble protein
Structural protein studies
Proprietà fisiche
Completamente inattivato dal calore al di sopra di 80 °C per 15-20 minuti.
Definizione di unità
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).
Nota sulla preparazione
Raccolto da brodo di coltura di S. griseus.
Risultati analitici
The protease is incubated for 10 minutes at pH 7.5 at 37°C in a 6 ml reaction volume containing 0.54% casein and 0.041 M potassium phosphate buffer. The reaction is stopped by the addition of 5.0 ml of 0.11 M trichloroacetic acid.
Altre note
This protease is completely inactivated by heating above 80°C for 15-20 minutes. This enzyme is more active at a higher pH range, showing the proteolytic activity even in 0.2N NaOH solution.
Bioscience, biotechnology, and biochemistry, 58(3), 470-474 (1994-03-01)
SAP, an extracellular alkaline serine protease produced by Streptomyces sp. YSA-130, was purified to homogeneity by CM-Sephadex column chromatography and crystallization. The enzyme was a monomeric protein with a molecular weight of 19,000 as estimated by SDS-PAGE and gel filtration.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 228, 61-67 (2018-12-07)
The understanding of muscle tissue formation and regeneration is essential for the development of therapeutic approaches to treat muscle diseases or loss of muscle mass and strength during ageing or cancer. One of the critical steps in muscle formation is
DYRK1A is a major causative gene in Down syndrome (DS). Reduced incidence of solid tumors such as neuroblastoma in DS patients and increased vascular anomalies in DS fetuses suggest a potential role of DYRK1A in angiogenic processes, but in vivo
Journal of animal science, 81(10), 2617-2627 (2003-10-14)
A dual-flow continuous culture system was used to investigate the effects of pH and addition of an enzyme mixture to a total mixed ration (TMR) on fermentation, nutrient digestion, and microbial protein synthesis. A 4 x 4 Latin square design
Journal of virology, 81(17), 8933-8943 (2007-06-15)
Dendritic cells (DCs) potently stimulate the transmission of human immunodeficiency virus type 1 (HIV-1) to CD4(+) T cells. Immature DCs (iDCs) located in submucosal tissues can capture HIV-1 and migrate to lymphoid tissues, where they become mature DCs (mDCs) for
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..