Anti-c-TEN (C-terminal) polyclonal antibody

The effects of cold storage and shelf life of 'Big Top,' 'Honey Blaze(cov),' 'Honey Royale(cov),' 'Venus,' 'August Red,' and 'Nectagala(cov)' nectarines were evaluated. Volatile compounds, firmness, soluble solids content, titratable acidity, color, and degree of consumer acceptance of the fruit were determined at harvest, after storage at -0.5 A degrees C for 10, 20, or 40 days and following 3 days at 20 A degrees C. Ten days cold storage plus 3 days at 20 A degrees C produced the highest total ester emission for 'Nectagala(cov)' and 'August Red,' while similar results were obtained after 10 days cold storage for the 'Big Top' and 'Honey Blaze(cov)' and 20 days cold storage for 'Honey Royale(cov)' and 'Venus.' For 'Nectagala(cov),' this higher total ester emission coincided with the greatest percentage of satisfied consumers. Increased consumer acceptance was associated with the cultivars and storage time that resulted in firmer fruits and greater concentrations of specific volatile compounds.

Vibrio extracellular metalloprotease (vEP), secreted from Vibrio vulnificus, shows various proteolytic function such as prothrombin activation and fibrinolytic activities. Premature form of vEP has an N-terminal (nPP) and a C-terminal (C-ter100) region. The nPP and C-ter100 regions are autocleaved for the matured metalloprotease activity. It has been proposed that two regions play a key role in regulating enzymatic activity of vEP. Especially, C-ten 100 has a regulatory function on proteolytic activity of vEP. C-ter100 domain has been cloned into the E. coli expression vectors, pET32a and pGEX 4T-1 with TEV protease cleavage site and purified using gel-filtration chromatography followed by affinity chromatography. To understand how C-ter100 modulates proteolytic activity of vEP, structural studies were performed by heteronuclar multi-dimensional NMR spectroscopy. Backbone H-1, N-15 and C-13 resonances were assigned by data from standard triple resonance and HCCH-TOCSY experiments. The secondary structures of vEP C-ter100 were determined by TALOS+ and CSI software based on hydrogen/deuterium exchange. NMR data show that C-ter 100 of vEP forms a beta-barrel structure consisting of eight beta-strands.