scholarly journals Functional and physical molecular size of the chicken hepatic lectin determined by radiation inactivation and sedimentation equilibrium analysis.

1990 ◽  
Vol 265 (7) ◽  
pp. 3744-3749
Author(s):  
C J Steer ◽  
J C Osborne ◽  
E S Kempner
Keyword(s):  
Molecular Size ◽  
Equilibrium Analysis ◽  
Sedimentation Equilibrium ◽  
Radiation Inactivation

Determination of the molecular size of the 5-HT3 receptor binding site by radiation inactivation

1989 ◽  
Vol 172 (6) ◽  
pp. 497-500 ◽  
Author(s):  
H. Gozlan ◽  
L.E. Schechter ◽  
F. Bolanos ◽  
M.B. Emerit ◽  
M.C. Miquel ◽  
...  
Keyword(s):  
Binding Site ◽  
Receptor Binding ◽  
Molecular Size ◽  
Receptor Binding Site ◽  
Radiation Inactivation

Molecular size of [3H]WB-4101-binding sites in rat cortex as determined by radiation inactivation

1985 ◽  
Vol 34 (20) ◽  
pp. 3617-3621
Author(s):  
Jette Rank ◽  
Thomas Breck ◽  
Annette Kibenich ◽  
Mogens Nielsen
Keyword(s):  
Binding Sites ◽  
Molecular Size ◽  
Rat Cortex ◽  
Radiation Inactivation ◽  
Wb 4101

scholarly journals The structure of L-lactate oxidase from Mycobacterium smegmatis

1977 ◽  
Vol 165 (2) ◽  
pp. 375-383 ◽  
Author(s):  
P A Sullivan ◽  
C Y Soon ◽  
W J Schreurs ◽  
J F Cutfield ◽  
M G Shepherd
Keyword(s):  
Electron Microscopy ◽  
Mycobacterium Smegmatis ◽  
Sedimentation Velocity ◽  
Equilibrium Analysis ◽  
Sedimentation Equilibrium ◽  
Cross Linking ◽  
Velocity Analysis ◽  
Approach To Equilibrium ◽  
Lactate Oxidase ◽  
Dimethyl Suberimidate

1. An improved purification was developed for L-lactate oxidase from Mycobacterium smegmatis. 2. The mol.wt. of the native enzyme by a sedimentation-equilibrium analysis was 345 000, and other ultracentrifuge methods gave values in the range 345 000-350 000. 3. An amino acid analysis, determinations of protein and flavin, a sedimentation-velocity analysis and an approach to equilibrium analysis gave values for the subunit mol.wt. in the range 43 500-47 000. 4. It was concluded that L-lactate oxidase contains eight subunits of mol.wt. 43 500. 5. Cross-linking of the subunits with dimethyl suberimidate and electron-microscopy studies were consistent with an octameric structure.

scholarly journals Isolation and properties of hyaluronic acid from bovine heart valves

1969 ◽  
Vol 113 (3) ◽  
pp. 559-563 ◽  
Author(s):  
F. A. Meyer ◽  
B. N. Preston ◽  
D. A. Lowther
Keyword(s):  
Hyaluronic Acid ◽  
Synovial Fluid ◽  
Heart Valves ◽  
Glucuronic Acid ◽  
Molecular Size ◽  
Sedimentation Equilibrium ◽  
Molar Ratio ◽  
Soluble Extract ◽  
Caesium Chloride ◽  
Bovine Heart

1. A soluble extract of bovine heart valves was obtained after the tissue had been pulverized at liquid-nitrogen temperatures in a mill. 2. Hyaluronic acid was isolated from the crude extract by sedimentation equilibrium in a caesium chloride density gradient (Franek & Dunstone, 1966). 3. Analysis of the product indicated that it contained 15% of protein and the molar ratio of glucuronic acid to glucosamine was 1·27. 4. Its physicochemical properties, as determined by lightscattering, viscosity and sedimentation studies, suggested that its molecular size and configuration were similar to those of hyaluronic acid isolated from ox synovial fluid (Preston, Davies & Ogston, 1965).

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