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A Domain Approach to the Adsorption of Complex Proteins: Preliminary Analysis and Application to Albumin

Joseph D. Andrade ; Department of Bioengineering, Center for Biopolymers at Interfaces, University of Utah, 2480 MEB, Salt Lake City, Utah 84112 USA
Vladimir Hlady ; Department of Bioengineering, Center for Biopolymers at Interfaces, University of Utah, 2480 MEB, Salt Lake City, Utah 84112 USA
Ai-Ping Wei ; Department of Bioengineering, Center for Biopolymers at Interfaces, University of Utah, 2480 MEB, Salt Lake City, Utah 84112 USA
Carl-Gustav Golander ; Department of Bioengineering, Center for Biopolymers at Interfaces, University of Utah, 2480 MEB, Salt Lake City, Utah 84112 USA


Puni tekst: engleski pdf 13.588 Kb

str. 527-538

preuzimanja: 296

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Sažetak

Albumin consists of three large domains with differences in electrostatic nature, charge-pH characteristics, and denaturability.
The interfacial activity of albumin is due, at least in part, to the mterfacial activity of its constituent domains. Consideration of the structure and interfacial activity of the various domains permits new and more precise hypotheses to be developed, with which new and better experiments can be designed. Such hypotheses allow one to evaluate and compare adsorption data, including kinetics and isotherms, adsorbed layer thickness, refractive index, lateral cohesion, multilayer formation, etc.
We feel strongly that each different protein is a unique molecular personality, which must be understood and considered if we are to more fully understand and apply the interfacial behavior of complex proteins.

Ključne riječi

Hrčak ID:

137389

URI

https://hrcak.srce.hr/137389

Datum izdavanja:

28.12.1990.

Posjeta: 668 *