Purification and characterization of a soluble, cytoplasmic decycling maltodextrinase from a Lactobacillus species, strain 26X, isolated from kitchen waste water

1995 ◽  
Vol 43 (5) ◽  
pp. 838-843
Author(s):  
H. Bender

The present study is about the analysis of sullage collected from Tiruvanchery region, Chennai, Tamil Nadu, India. Sullage is the waste water from households, sinks, bathrooms, kitchen households but except the waste water from toilets. In this project, 6 samples of waste water were collected in 3 different apartments. The apartments are Ruby Grand, Ruby Regency and Green Paradise. The 2 samples of the waste water are the kitchen waste water and washing clothes waste water. Physical, chemical and biological parameters are tested in environmental laboratory. The chemical parameters were tested using titrimetric method. It is found that all samples were safe against pH, Alkalinity, Flouride, Chloride, Iron, Phosphate, and Turbidity which are within the permissible limits of IS3306 (1974)


1994 ◽  
Vol 92 (3) ◽  
pp. 479-486 ◽  
Author(s):  
Cynthia M. Galloway ◽  
W. Mack Dugger

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi

SummaryTissue-type plasminogen activator (TPA) was purified from maxillary mucosa with chronic inflammation and compared with urokinase. Purification procedure consisted of the extraction from delipidated mucosa with 0.3M potassium acetate buffer (pH 4.2), 66% saturation of ammonium sulfate, zinc chelate-Sepharose, concanavalin A-Sepharose and Sephadex G-100 gel filtration chromatographies.The molecular weight of the TPA was approximately 58,000 ± 3,000. Its activity was enhanced in the presence of fibrin and was quenched by placental urokinase inhibitor, but not quenched by anti-urokinase antibody. The TPA made no precipitin line against anti-urokinase antibody, while urokinase did.All these findings indicate that the TPA in maxillary mucosa with chronic inflammation is immunologically dissimilar to urokinase and in its affinity for fibrin.


1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.


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