Purification and characterization of fucose-containing sulphated polysaccharides from Sargassum tenerrimum and their biological activity

2019 ◽  
Vol 31 (5) ◽  
pp. 3101-3113
Author(s):  
Manoj Saravana Guru Mohan ◽  
Anant Achary ◽  
Vasanthi Mani ◽  
Eduardas Cicinskas ◽  
Aleksandra A. Kalitnik ◽  
...  
Keyword(s):  
Biological Activity ◽  
Purification And Characterization ◽  
Sulphated Polysaccharides ◽  
Sargassum Tenerrimum

scholarly journals Purification and characterization of guinea-pig intestinal brush borders

1975 ◽  
Vol 152 (1) ◽  
pp. 157-159 ◽  
Author(s):  
K Andersen ◽  
G V Lippe ◽  
L Morkrid ◽  
H Schjonsby
Keyword(s):  
Biological Activity ◽  
Guinea Pig ◽  
Gradient Centrifugation ◽  
Fold Increase ◽  
Prolonged Storage ◽  
Purification And Characterization ◽  
Brush Borders ◽  
Centrifugation Step ◽  
Vitamin B 12

The purification of guinea-pig intestinal brush borders by a rapid sucrose-gradient-centrifugation step is reported. A 29-fold increase in the maltase/DNA quotient indicates considerable purification of the brush borders from nuclei. The biological activity of the brush borders was well preserved, as demonstrated by a high recovery of human gastric-juice-mediated uptake of 57Co-labelled vitamin B-12; homogeneity and purity were confirmed by scanning electron microscopy. Both the morphological appearance and biological activity were unchanged after prolonged storage in glycerol.

scholarly journals Purification and Characterization of a Monooxygenase Involved in the Biosynthetic Pathway of the Antitumor Drug Mithramycin

2003 ◽  
Vol 185 (13) ◽  
pp. 3962-3965 ◽  
Author(s):  
David Rodríguez ◽  
Luis M. Quirós ◽  
Alfredo F. Braña ◽  
José A. Salas
Keyword(s):  
Biological Activity ◽  
Biosynthetic Pathway ◽  
Flavin Adenine Dinucleotide ◽  
Chain Molecule ◽  
Aliphatic Chain ◽  
Purification Procedure ◽  
Reaction Products ◽  
Purification And Characterization ◽  
Optimal Ph

ABSTRACT A monooxygenase encoded by the mtmOIV gene from the mithramycin gene cluster of Streptomyces argillaceus was purified 21-fold by a three-step purification procedure. This monooxygenase catalyzes the oxidative cleavage of the fourth ring of premithramycin B. The enzyme was dependent on NADPH and flavin adenine dinucleotide for activity with optimal pH at 9.5, and the Km values for NADPH and premithramycin B were 269.22 and 23.35 μM, respectively. The reaction catalyzed by MtmOIV yields two possible isomers of the same basic shortened aliphatic chain molecule. One of the reaction products showed important biological activity, thus highlighting the importance of the cleavage of the fourth ring of the aglycon for biological activity.

Purification and characterization of phosphoglucomutase from peas

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

Purification and Characterization of Tissue-Type Plasminogen Activator in Maxillary Mucosa with Chronic Inflammation

1985 ◽  
Vol 54 (02) ◽  
pp. 485-489 ◽  
Author(s):  
Yukiyoshi Hamaguchi ◽  
Masuichi Ohi ◽  
Yasuo Sakakura ◽  
Yasuro Miyoshi
Keyword(s):  
Plasminogen Activator ◽  
Chronic Inflammation ◽  
Gel Filtration ◽  
Potassium Acetate ◽  
Tissue Type ◽  
Purification And Characterization ◽  
Tissue Type Plasminogen Activator ◽  
Urokinase Inhibitor ◽  
Type Plasminogen Activator

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.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

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.

Fabrication and Characterization of Polyoxometalate based Nano-hybrids: Evaluation of their role in Biological Activity

2019 ◽  
Vol 35 (4) ◽  
pp. 475-484
Author(s):  
SHIVA ARUN ◽  
◽  
PRABHA BHARTIYA ◽  
AMREEN NAZ ◽  
SUDHEER RAI ◽  
...  
Keyword(s):  
Biological Activity ◽  
Fabrication And Characterization
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