Purification and characterization of hydrolysable tannins extracted from Coriaria nepalensis bark using macroporous resin and their application in gallic acid production

2021 ◽  
Vol 162 ◽  
pp. 113302
Author(s):  
Linxin Guo ◽  
Taotao Qiang ◽  
Yangmin Ma ◽  
Longfang Ren ◽  
Tingting Dai
Keyword(s):  
Gallic Acid ◽  
Acid Production ◽  
Macroporous Resin ◽  
Purification And Characterization ◽  
Hydrolysable Tannins

scholarly journals Purification and Characterization of Gallic Acid Decarboxylase from Pantoea agglomerans T71

1998 ◽  
Vol 64 (12) ◽  
pp. 4743-4747 ◽  
Author(s):  
Mitsuhiro Zeida ◽  
Marco Wieser ◽  
Toyokazu Yoshida ◽  
Tsuyoshi Sugio ◽  
Toru Nagasawa
Keyword(s):  
Gallic Acid ◽  
Cell Extract ◽  
Spectrophotometric Analysis ◽  
Acid Decarboxylase ◽  
Purification And Characterization ◽  
Resting Cell ◽  
Oxygen Sensitive ◽  
A Cell ◽  
Plasma Emission Spectroscopy

ABSTRACT Oxygen-sensitive gallic acid decarboxylase from Pantoea(formerly Enterobacter) agglomerans T71 was purified from a cell extract after stabilization by reducing agents. This enzyme has a molecular mass of approximately 320 kDa and consists of six identical subunits. It is highly specific for gallic acid. Gallic acid decarboxylase is unique among similar decarboxylases in that it requires iron as a cofactor, as shown by plasma emission spectroscopy (which revealed an iron content of 0.8 mol per mol of enzyme subunit), spectrophotometric analysis (absorption shoulders at 398 and 472 nm), and inhibition of the enzyme activity by 2,2′-bipyridyl, o-phenanthroline, and EDTA. Another interesting feature of this strain is the fact that it contains a tannase, which is used together with the gallic acid decarboxylase in a two-enzyme resting cell bioconversion to synthesize valuable pyrogallol from readily available tannic acid.

Macroporous resin purification and characterization of flavonoids from Platycladus orientalis (L.) Franco and their effects on macrophage inflammatory response

2017 ◽  
Vol 8 (1) ◽  
pp. 86-95 ◽  
Author(s):  
Jiaoyan Ren ◽  
Yamei Zheng ◽  
Zehua Lin ◽  
Xin Han ◽  
Wenzhen Liao
Keyword(s):  
Inflammatory Response ◽  
Macroporous Resin ◽  
Purification And Characterization ◽  
Platycladus Orientalis ◽  
Macrophage Cells ◽  
Inflammatory Mechanism ◽  
Anti Inflammatory

LPS-induced macrophage cells as a model of inflammatory response to investigate the anti-inflammatory mechanism of the purifiedPlatycladus orientalis(L.) Franco flavonoids.

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.

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