Optimization and kinetic studies of photodegradation of Rhodamine B with immobilized Ag-, S-, and N-doped TiO2 under visible irradiation: using Box–Behnken designs (BBDs), multivariate curve resolution (MCR-ALS) and parallel factor (PARAFAC) analysis

2016 ◽  
Vol 8 (21) ◽  
pp. 4293-4299 ◽  
Author(s):  
H. Khalilian ◽  
A. Semnani ◽  
Å. Rinnan ◽  
H. Haddadi
Keyword(s):  
Rhodamine B ◽  
Kinetic Studies ◽  
Multivariate Curve Resolution ◽  
Two Stage ◽  
Doped Tio2 ◽  
Curve Resolution ◽  
Parallel Factor ◽  
Visible Irradiation

This study is based on a two-stage approach.

Kinetic studies of nitrofurazone photodegradation by multivariate curve resolution applied to UV-spectral data

2010 ◽  
Vol 386 (1-2) ◽  
pp. 99-107 ◽  
Author(s):  
Michele De Luca ◽  
Sílvia Mas ◽  
Giuseppina Ioele ◽  
Filomena Oliverio ◽  
Gaetano Ragno ◽  
...  
Keyword(s):  
Spectral Data ◽  
Kinetic Studies ◽  
Multivariate Curve Resolution ◽  
Curve Resolution

Factor V from Human Plasma

1961 ◽  
Vol 05 (01) ◽  
pp. 001-020
Author(s):  
Douglas M. Surgenor ◽  
Nancy A. Wilson ◽  
Anne S. Henry
Keyword(s):  
Human Serum ◽  
Human Plasma ◽  
Kinetic Data ◽  
Human Factor ◽  
Kinetic Studies ◽  
Partial Purification ◽  
Factor V ◽  
Two Stage ◽  
Plasma Factor ◽  
Tissue Thromboplastin

SummaryA method is described for the partial purification of a human plasma factor which accelerates the conversion of prothrombin to thrombin in the presence of tissue thromboplastin. This factor may be dried from the frozen state, and may be kept in stable dry form for long periods of time. The quantitative assay of this activity is done in a classical two-stage prothrombin system using tissue thromboplastin and calcium. From its properties, it is concluded that this activity corresponds to factor V, labile factor and plasma Ac-globulin.Chemical and kinetic studies reveal that human factor V is active in plasma and is destroyed by thrombin. Human serum has little or no factor V activity.These results thus fail to support the postulated activation of factor V during clotting. All of the kinetic data are consistent with an enzymatic role for factor V in the formation of tissue prothrombin activator (thromboplastin).

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