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KCATKorea City Air Terminal (Seoul, South Korea)
KCATKobe City Air Terminal (Japan)
KCATKansas City Actors Theatre (Kansas City, MO)
KCATKilkenny Collective for Arts Talent (Kilkenny, Ireland)
KCATKidney Check Australia Taskforce (est. 2001; Australia)
KCATOverall Enzymatic Catalytic Rate
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References in periodicals archive ?
The Michaelis-Menton plot for CueO activity using DMP as substrate gave Km value of 0.2umol, Kcat 0.68 S-1 and Kcat/km 1.2S-1uM-1.
Theoretical kinetic values of the purified enzyme Km Vmax Kcat (mg/mL) (gmol/min/mg) ([s.sup.-1]) 14.6 [+ or -] 2.33 47.4 [+ or -] 6.63 100.3 [+ or -] 14.05 Km Kcat/Km (mg/mL) (mL/mg/s) 14.6 [+ or -] 2.33 6.89 [+ or -] 0.118 All assays were performed in triplicate.
Type of Km (nM) Kcat ([min.sup.-1]) Kcat/Km protein ([min.sup.-1] x [micro][M.sup.-1]) TDG 0.72 0.042 58.5 SMUG1 2.63 0.011 4.2
This arrangement, Rensenhouse says, is "respected and supported by our community [board] members because they recognize that KCAT's real strength is its artistic integrity." Founding member Walter Coppage echoes the point, noting that the company's success comes from its commitment to being an "artist-led collective that brings a roundtable approach to choosing seasons and making artistic decisions."
The careers advice service is helping to promote KCAT by spreading the word and putting up posters.
n PROBABLY one of the most requested tunes at the moment is Destiny from Delinquent featuring KCat. The singer on this track, KCat, has honed her craft over a long period of time, she even won the inter-college talent contest, a title previously held by Daniel and Natasha Bedingfield.
The kinetic constants, kcat and kcat/Km, were found to be very similar between the angalogs, but much smaller than the authentic anthracyclines.
be sofo shel davar hi sipra al ha gneva la horim shela ve hem ba hatxala kcat ka'asu aval hevinu she hi mictaeret al ze [CP4] `Eventually she told her parents about the theft and they were a bit mad at the beginning but (they) understood that she was sorry about it' [CP4] b.
The H84C and H89C both bind 1 molZn(II)/mole enzyme, and the Kcat value for H89C, 33 +/- 4s-1 is significantly different from the wild type L 1 enzyme.
This paper presents an undergraduate laboratory exercise that allows for the experimental determination of the typical enzyme-kinetics parameters [the Michaelis constant (KM), the maximum rate of the enzyme-catalyzed reaction (Vmax), the turnover number (kcat), and the catalytic efficiency of the enzyme system at low substrate concentrations (kcat/KM)] using a standard benchtop multi-cell UV-vis spectrophotometer.
The kcat kinetic parameter was determined using some common acetylated substrates and the values.
However, the values of kcat and Vmax of the free urease were higher than that of immobilized urease.