Comparison of three distinct ELLA protocols for determination of apparent affinity constants between Con A and glycoproteins

2012 ◽  
Vol 94 ◽  
pp. 163-169 ◽  
Author(s):  
D. Mislovičová ◽  
J. Katrlík ◽  
E. Paulovičová ◽  
P. Gemeiner ◽  
J. Tkac
Keyword(s):  
Con A ◽  
Apparent Affinity ◽  
Affinity Constants

scholarly journals Fabrication of Carbohydrate Chips Based on Polydopamine for Real-Time Determination of Carbohydrate–Lectin Interactions by QCM Biosensor

Polymers ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 1275 ◽  
Author(s):  
Kun Shang ◽  
Siyu Song ◽  
Yaping Cheng ◽  
Lili Guo ◽  
Yuxin Pei ◽  
...  
Keyword(s):  
Real Time ◽  
Con A ◽  
Quartz Crystals ◽  
Ulex Europaeus ◽  
Novel Approach ◽  
Ulex Europaeus Agglutinin I ◽  
Flow Through ◽  
Time Determination ◽  
Kinetics Of

A novel approach for preparing carbohydrate chips based on polydopamine (PDA) surface to study carbohydrate–lectin interactions by quartz crystal microbalance (QCM) biosensor instrument has been developed. The amino-carbohydrates were immobilized on PDA-coated quartz crystals via Schiff base reaction and/or Michael addition reaction. The resulting carbohydrate-chips were applied to QCM biosensor instrument with flow-through system for real-time detection of lectin–carbohydrate interactions. A series of plant lectins, including wheat germ agglutinin (WGA), concanavalin A (Con A), Ulex europaeus agglutinin I (UEA-I), soybean agglutinin (SBA), and peanut agglutinin (PNA), were evaluated for the binding to different kinds of carbohydrate chips. Clearly, the results show that the predicted lectin selectively binds to the carbohydrates, which demonstrates the applicability of the approach. Furthermore, the kinetics of the interactions between Con A and mannose, WGA and N-Acetylglucosamine were studied, respectively. This study provides an efficient approach to preparing carbohydrate chips based on PDA for the lectin–carbohydrate interactions study.

Low Affinity Calcium Binding Sites of the Calcium Transport ATPase of Sarcoplasmic Reticulum Membranes

1980 ◽  
Vol 35 (11-12) ◽  
pp. 1012-1018 ◽  
Author(s):  
Wilhelm Hasselbach ◽  
Vera Koenig
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Binding Sites ◽  
Calcium Binding ◽  
Calcium Transport ◽  
External Surface ◽  
Transport Atpase ◽  
Affinity Constants ◽  
Calcium Binding Sites ◽  
Short Time

Calcium binding sites having low affinity constants of < 103 ᴍ-1 were titrated in native sarcoplasmic reticulum vesicles as well as in lipid deprived membranes and in the isolated calcium transport ATPase. Short time calcium binding measurements and the determination of the calcium binding heat allow to distinguish low affinity calcium binding sites located on the external surface of the sarcoplasmic reticulum membranes from those present in the section of the transport molecule directed to the vesicular space. The same number of internal binding sites was found for preparations deprived of their lipid content as well as of preparations depleted of their lipids and of their accessorial proteins. Magnesium interferes with calcium binding to the external as well as to the internal low affinity calcium binding sites. The implications of the existence of the low affinity calcium binding sites in the internal section of the calcium transport ATPase are discussed.

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