Sugar binding properties of various metal ion induced conformations in concanavalin A

Biochemistry ◽  
1978 ◽  
Vol 17 (11) ◽  
pp. 2169-2173 ◽  
Author(s):  
A. D. Sherry ◽  
A. E. Buck ◽  
C. A. Peterson
1973 ◽  
Vol 248 (2) ◽  
pp. 549-556
Author(s):  
Geoffrey H. McKenzie ◽  
William H. Sawyer

2001 ◽  
Vol 79 (4) ◽  
pp. 370-376 ◽  
Author(s):  
Catherine Morlay ◽  
Yolande Mouginot ◽  
Monique Cromer ◽  
Olivier Vittori

The possible removal of copper(II), nickel(II), or lead(II) by an insoluble crosslinked poly(acrylic acid) was investigated in dilute aqueous solution. The binding properties of the polymer were examined at pH = 6.0 or 4.0 with an ionic strength of the medium µ = 0.1 or 1.0 M (NaNO3) using differential pulse polarography as an investigation means. The highest complexing capacity of the polyacid was obtained with lead(II) at pH = 6.0 with µ = 0.1 M, 4.8 mmol Pb(II)/g polymer. The conditional stability constants of the complex species formed were determined using the method proposed by Ruzic assuming that only the 1:1 complex species was formed; for lead(II) at pH = 6.0 and µ = 0.1 M, log K' = 5.3 ± 0.2. It appeared that the binding properties of the polymer increased, depending on the metal ion, in the following order: Ni(II) < Cu(II) < Pb(II). The complexing capacity and log K' values decreased with the pH or with an increase of the ionic strength. These results were in agreement with the conclusions of our previous studies of the hydrosoluble linear analogues. Finally, with the insoluble polymer, the log K' values were comparable to those previously obtained with the linear analogue whereas the complexing capacity values expressed in mmol g-1 were slightly lower.Key words: insoluble crosslinked poly(acrylic acid), copper(II), nickel(II), and lead(II) complexation.


1987 ◽  
Vol 248 (1) ◽  
pp. 167-171 ◽  
Author(s):  
Y Hiller ◽  
J M Gershoni ◽  
E A Bayer ◽  
M Wilchek

A commercially available, purified preparation of avidin was found to comprise two polypeptide bands (Mr 18,000 and Mr 15,500 respectively). Both bands bound biotin as assessed by biotin overlays of protein blots. The Mr 15,500 polypeptide was found to differ from the Mr 18,000 polypeptide only in its sugar content. When the commercial preparation was applied to a concanavalin A affinity column, the glycosylated forms were retarded as expected, and homotypic nonglycosylated avidin tetramers which failed to bind selectively to the column were collected in the effluent. The biotin-binding properties of the nonglycosylated avidin were equivalent to those obtained for the native (glycosylated) avidin molecule, indicating that the oligosaccharide moiety is not essential for the binding activity.


Biochemistry ◽  
1978 ◽  
Vol 17 (21) ◽  
pp. 4425-4430 ◽  
Author(s):  
Douglas J. Christie ◽  
Gerald M. Alter ◽  
James A. Magnuson

Biochemistry ◽  
1973 ◽  
Vol 12 (10) ◽  
pp. 1914-1917 ◽  
Author(s):  
Menahem Shoham ◽  
A. Joseph Kalb ◽  
Israel Pecht
Keyword(s):  

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