Biochemical and spectroscopic characterization of the high molecular weight cytochrome c from Desulfovibrio vulgaris Hildenborough expressed in Desulfovibrio desulfuricans G200

Biochemistry ◽  
1992 ◽  
Vol 31 (12) ◽  
pp. 3281-3288 ◽  
Author(s):  
Mireille Bruschi ◽  
Patrick Bertrand ◽  
Claude More ◽  
Gisele Leroy ◽  
Jacques Bonicel ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
High Molecular Weight ◽  
Desulfovibrio Desulfuricans ◽  
Spectroscopic Characterization ◽  
Desulfovibrio Vulgaris ◽  
Desulfovibrio Vulgaris Hildenborough

Crystallization And Mad Data Collection Of High-Molecular Weight Cytochrome C From Desulfovibrio Vulgaris Miyazaki F

2004 ◽  
Vol 11 (1) ◽  
pp. 93-96
Author(s):  
Naoki Shibata ◽  
Kyoko Suto ◽  
Eiko Ichimura ◽  
Kazutaka Yoshimura ◽  
Kenji Muneo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Data Collection ◽  
High Molecular Weight ◽  
Desulfovibrio Vulgaris

Axial coordination and reduction potentials of the 16 hemes in high-molecular-weight cytochrome c from Desulfovibrio vulgaris

1993 ◽  
Vol 51 (1-2) ◽  
pp. 28 ◽  
Author(s):  
W.R. Hagen ◽  
M.F.J.M. Verhagen ◽  
A.J. Pierik ◽  
R.B.G. Wolbert ◽  
L.F. Mallée ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
High Molecular Weight ◽  
Desulfovibrio Vulgaris ◽  
Axial Coordination ◽  
Reduction Potentials

Rapid Isolation of High Molecular Weight Urokinase from Native Human Urine

1982 ◽  
Vol 47 (03) ◽  
pp. 197-202 ◽  
Author(s):  
Kurt Huber ◽  
Johannes Kirchheimer ◽  
Bernd R Binder
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Human Urine ◽  
Gel Filtration ◽  
Chain Structure ◽  
The Other ◽  
Single Chain ◽  
Apparent Homogeneity ◽  
Sequential Adsorption

SummaryUrokinase (UK) could be purified to apparent homogeneity starting from crude urine by sequential adsorption and elution of the enzyme to gelatine-Sepharose and agmatine-Sepharose followed by gel filtration on Sephadex G-150. The purified product exhibited characteristics of the high molecular weight urokinase (HMW-UK) but did contain two distinct entities, one of which exhibited a two chain structure as reported for the HMW-UK while the other one exhibited an apparent single chain structure. The purification described is rapid and simple and results in an enzyme with probably no major alterations. Yields are high enough to obtain purified enzymes for characterization of UK from individual donors.

Preparation and Characterization of the High Molecular Weight [3H]Hyaluronic Acid

1992 ◽  
Vol 57 (10) ◽  
pp. 2151-2156 ◽  
Author(s):  
Peter Chabreček ◽  
Ladislav Šoltés ◽  
Hynek Hradec ◽  
Jiří Filip ◽  
Eduard Orviský
Keyword(s):  
Molecular Weight ◽  
Hyaluronic Acid ◽  
High Molecular Weight ◽  
Methyl Bromide ◽  
High Performance ◽  
Hydrogen Atoms ◽  
Isolation And Characterization ◽  
Labelling Procedure ◽  
Enzymatic Depolymerization

Two methods for the preparation of high molecular weight [3H]hyaluronic acid were investigated. In the first one, hydrogen atoms in the molecule were replaced by tritium. This isotopic substitution was performed in aqueous solution using Pd/CaCO3 as the catalyst. In the second method, the high molecular weight hyaluronic acid was alkylated with [3H]methyl bromide in liquid ammonia at a temperature of -33.5 °C. High-performance gel permeation chromatographic separation method was used for the isolation and characterization of the high molecular weight [3H]hyaluronic acid. Molecular weight parameters for the labelled biopolymers were Mw = 128 kDa, Mw/Mn = 1.88 (first method) and Mw = 268 kDa, Mw/Mn = 1.55 (second method). The high molecular weight [3H]hyaluronic acid having Mw = 268 kDa was degraded further by specific hyaluronidase. Products of the enzymatic depolymerization were observed to be identical for both, labelled and cold biopolymer. This finding indicates that the described labelling procedure using [3H]methyl bromide does not induce any major structural rearrangements in the molecule.

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