Purification and characterization of biologically active 1,4-linked α-d-oligogalacturonides after partial digestion of polygalacturonic acid with endopolygalacturonase

1993 ◽  
Vol 247 ◽  
pp. 9-20 ◽  
Author(s):  
Mark D. Spiro ◽  
Keith A. Kates ◽  
Alan L. Koller ◽  
Malcolm A. O'Neill ◽  
Peter Albersheim ◽  
...  
Keyword(s):  
Biologically Active ◽  
Polygalacturonic Acid ◽  
Purification And Characterization ◽  
Partial Digestion

Purification and characterization of tuberculin-active components from BCG

1975 ◽  
Vol 21 (12) ◽  
pp. 2019-2027
Author(s):  
M. Laguerre ◽  
R. Turcotte
Keyword(s):  
Physicochemical Properties ◽  
Guinea Pigs ◽  
Gel Filtration ◽  
Biologically Active ◽  
Polyacrylamide Gels ◽  
Active Components ◽  
Purification And Characterization ◽  
Molecular Weights ◽  
Antigenic Activity

The tuberculin activity of protoplasmic extracts isolated from living BCG was purified successively by gel filtration on Sephadex G-100 and G-75, and by electrophoresis on 7.5% and on gradient (6–18%) polyacrylamide gels. The tuberculin-active fractions, as determined in BCG-sensitized guinea pigs, were used as the starting material for each of the following fractionation steps.The physicochemical properties and the antigenic activity of the biologically active fractions have shown that a single component, or only a few ones with similar properties, possessed high tuberculin activity. These active components were proteins having relatively high molecular weights (about 72 000) and could behave as antigens.

Production, purification and characterization of biologically active recombinant human nerve growth factor

1990 ◽  
Vol 171 (1) ◽  
pp. 116-122 ◽  
Author(s):  
Makoto Iwane ◽  
Yumiko Kitamura ◽  
Yoshihiko Kaisho ◽  
Koji Yoshimura ◽  
Asae Shintani ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Biologically Active ◽  
Purification And Characterization ◽  
Nerve Growth ◽  
Human Nerve

scholarly journals Purification and characterization of an L-glutamic acid60-L-alanine30-L-tyrosine10 (GAT)-specific suppressor factor from genetic responder mice.

1983 ◽  
Vol 158 (4) ◽  
pp. 1034-1047 ◽  
Author(s):  
C M Sorensen ◽  
C W Pierce ◽  
D R Webb
Keyword(s):  
Specific Activity ◽  
Reversed Phase ◽  
Biologically Active ◽  
Reversed Phase Hplc ◽  
Purification And Characterization ◽  
Suppressor Factor ◽  
Chemical Homogeneity ◽  
T Cell Factor ◽  
Molecular Weights

A hybridoma-derived, GAT-specific suppressor T cell factor (GAT-TsFR) from responder C57BL/10 mice has been purified to apparent chemical homogeneity using reversed phase HPLC techniques. 40 l of starting material yielded approximately 880 micrograms protein with a specific activity of 28.4 X 10(3) S50 U/ng protein representing a purification factor of 4.2 X 10(6). Purified GAT-TsFR is a hydrophobic protein with a minimum molecular weight of 18,000 that is capable of forming biologically active aggregates with molecular weights of 28,000, 64,000 and approximately 84,000 and has a pI of 6.4. GAT-TsFR is a glycoprotein that binds GAT and GT, but not GA, and bears determinants encoded by the I-J subregion of the H-2 complex. This GAT-TsFR derived from an H-2b responder haplotype to GAT is compared with GAT-TsF derived from the nonresponder H-2q haplotype on the basis of biochemical and some serological properties.

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