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The Adsorption of Bovine Blood Proteins Onto the Surface of O-(carboxymethyl)chitin

The Adsorption of Bovine Blood Proteins Onto the Surface of O-(carboxymethyl)chitin

S Nishimura, Y Ikeuchi, S Tokura

Carbohydr Res. 1984 Dec 1;134(2):305-12.

PMID: 6085030

Abstract:

Chitin was found to interact with bovine blood proteins and the affinities of these proteins for chitin tended to be decreased by the introduction of O-carboxymethyl (CM) groups onto the chitin surface, especially with fibrinogen. As the adsorption of blood proteins to the CM-chitin (d.s. 0.35) was assumed to follow an isothermal adsorption-curve, the adsorption coefficients were estimated by applying the Langmuir equation. Bovine serum albumin showed the highest affinity among the proteins applied in this experiment [KBSA (bovine serum albumin); 20.0, KB gamma G (bovine gamma globulin); 1.96, KBF (bovine fibrinogen); 1.20]. The binding site of BSA for CM-chitin was assumed to be regulated not only by the cationic groups of BSA but also by other factors such as the recognition capacity of BSA to bind to GlcNAc residues in CM-chitin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9007834	γ-Globulins from bovine blood		9007-83-4	Price

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