𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Adsorption Dynamics of Native and Alkylated Derivatives of Bovine Serum Albumin at Air–Water Interfaces

✍ Scribed by Daechul Cho; Ganesan Narsimhan; Elias I. Franses

Publisher
Elsevier Science
Year
1996
Tongue
English
Weight
193 KB
Volume
178
Category
Article
ISSN
0021-9797

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Adsorption Dynamics of Native and Pentyl
Adsorption Dynamics of Native and Pentylated Bovine Serum Albumin at Air–Water Interfaces: Surface Concentration/ Surface Pressure Measurements
✍ Daechul Cho; Ganesan Narsimhan; Elias I. Franses 📂 Article 📅 1997 🏛 Elsevier Science 🌐 English ⚖ 339 KB

native and pentylated BSA of different surface hydrophobicphobicity; air-water interface. ities. The P-G relationship during the dynamics of adsorption is compared with the adsorption isotherm of spread monolayer. The dynamic P-G relationship is found to be

Structural Conformation of Bovine Serum
Structural Conformation of Bovine Serum Albumin Layers at the Air–Water Interface Studied by Neutron Reflection
✍ J.R. Lu; T.J. Su; R.K. Thomas 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 294 KB

The adsorption of bovine serum albumin (BSA) at the air-water interface has been studied by specular neutron reflection. The variation of the adsorbed amount and the total thickness of the BSA layer with respect to bulk BSA concentration was determined at pH 5, close to its isoelectric point (IP). W

Adsorption Dynamics of α-Lactalbumin and
Adsorption Dynamics of α-Lactalbumin and β-Lactoglobulin at Air–Water Interfaces
✍ Michel Cornec; Daechul Cho; Ganesan Narsimhan 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 149 KB

Dynamics of adsorption of 14 C radiolabeled ␤-lactoglobulin and ␣-lactalbumin at the air-water interface was investigated through the measurement of surface pressure () and surface concentration (⌫) via a radiotracer technique. Adsorption was diffusion controlled at short times, the rates of increas

Adsorption Kinetics and Elutability of α
Adsorption Kinetics and Elutability of α-Lactalbumin, β-Casein, β-Lactoglobulin, and Bovine Serum Albumin at Hydrophobic and Hydrophilic Interfaces
✍ Viwat Krisdhasima; Pravina Vinaraphong; Joseph McGuire 📂 Article 📅 1993 🏛 Elsevier Science 🌐 English ⚖ 494 KB

Adsorption kinetic data recorded for \(\alpha\)-lactalbumin, \(\beta\)-casein, \(\beta\)-lactoglobulin, and bovine serum albumin at silanized silica surfaces of low and high hydrophobicity, along with the surfactant-mediated elutability of each from hydrophobic silica, were interpreted with referenc