Partial purification and further characterization of the novel endoglucosaminidase from human serum that hydrolyses 4-methylumbelliferyl-N-acetyl-β-d-chitotetraoside (MU-TACT hydrolase)

1994 ◽  
Vol 26 (12) ◽  
pp. 1369-1375 ◽  
Author(s):  
B. Overdijk ◽  
G.J. Van Steijn ◽  
W.R. Den Tandt
Keyword(s):  
Human Serum ◽  
Partial Purification ◽  
The Novel

Partial purification, characterization and wheat bran degradation studies of a new phytase from the Bacillus megaterium EBD 9-1 strain

2017 ◽  
Vol 42 (3) ◽  
Author(s):  
Elif Demirkan ◽  
Tuba Sevgi ◽  
Dilara Akcakoca ◽  
Figen Ersoy
Keyword(s):  
Gel Filtration ◽  
Partial Purification ◽  
The Novel ◽  
Bacterial Identification ◽  
Ammonium Sulfate Precipitation ◽  
16S Rrna Analysis ◽  
Sequence Identity ◽  
And Storage ◽  
Identification And Characterization

AbstractObjective:The present study was designed to report the bacterial identification and characterization of a new phytase enzyme from aMethods:sp. strain was identified based on 16S rRNA analysis. The phytase was partially purified through ammonium sulfate precipitation and Sephadex G100 gel filtration steps, and characterized for its activity and stability.Results:The new isolate EBD 9-1 showed 100% sequence identity withConclusion:Consequently, due to the characteristics such as significant stability at higher temperatures, alkaline pH and storage of the novel phytase enzyme produced by

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

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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