scholarly journals The thermodynamics of interaction between Sephadex and penetrating solutes

1970 ◽  
Vol 116 (2) ◽  
pp. 171-175 ◽  
Author(s):  
A. G. Ogston ◽  
Panee Silpananta
Keyword(s):  
Phase Separation ◽  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Partition Coefficients ◽  
Virial Coefficients

1. We have measured the partition coefficients of bovine serum albumin with Sephadex grades G-100, G-150 and G-200, and of a dextran ([unk]n 19700) and a polyethylene glycol ([unk]n 8000) with Sephadex G-200. We have also measured the effects of these solutes on the inner volumes of the grades of Sephadex. 2. The results can be described with fair consistency by means of a simple thermodynamic treatment that makes use of the virial coefficients of Sephadex and of the solute, and of a coefficient that expresses their interaction. This coefficient is related to the ‘exclusion volume’ of Sephadex for the solutes. 3. The Sephadex G-200–polyethylene glycol system shows anomalies of behaviour that are ascribed to the occurrence of ‘incompatible’ phase separation within the Sephadex beads.

Human corticotropin (ACTH) radioimmunoassay with synthetic 1--24 ACTH.

1979 ◽  
Vol 25 (7) ◽  
pp. 1267-1273 ◽  
Author(s):  
P C Kao ◽  
N S Jiang ◽  
P C Carpenter
Keyword(s):  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Confidence Limit ◽  
Normal Subjects ◽  
Cross Reactivity ◽  
Normal Range ◽  
Beta Endorphin

Abstract A corticotropin antiserum was obtained from rabbits immunized with synthetic 1--24 corticotropin conjugated with bovine serum albumin. The antiserum did not cross react with synthetic alpha-melanotropin or with synthetic beta-endorphin and had a cross reactivity of 0.23% with human beta-lipotropin. We developed a radioimmunoassay with the antiserum obtained, in which we used polyethylene glycol in conjunction with a second precipitating antibody for fast (15-min) separation of antibody-bound and free corticotropin. The assay had a sensitivity of 16 ng/L and was validated on patients with various pituitary and adrenal diseases. From 103 normal subjects, the median value for corticotropin in specimens collected during the morning was 34 ng/L of plasma; the upper 95% confidence limit of the normal range was 98 ng/L.

Structural analysis of poplar and Masson pine lignocresols and comparison of their bovine serum albumin adsorption characteristics

TAPPI Journal ◽  
2019 ◽  
Vol 18 (01) ◽  
pp. 31-43
Author(s):  
Lulu Zhu ◽  
Zhang Feng ◽  
Dongliang Xu ◽  
Guigan Fang ◽  
Hao Ren
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Phase Separation ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Proton Nuclear Magnetic Resonance ◽  
Masson Pine ◽  
Nuclear Magnetic

In this study, poplar and Masson pine trees were used as raw materials to examine the structural characteristics of lignin that had been isolated with a phase separation system. Following phase separation, the structure of lignocresol (LC) was characterized with Fourier transform infrared (FTIR) spectroscopy, high-performance gel permeation chromatography (GPC), proton nuclear magnetic resonance (1H-NMR) spectroscopy, and two-dimensional heteronuclear single quantum coherence nuclear magnetic resonance (2D HSQC NMR) spectroscopy. Phase separation made it possible to analyze the proportions and the differences between various structural units in the isolated lignin, as well as the types of linkages between them. In-situ and real-time monitoring of the adsorption and desorption properties of the LC membranes were conducted with a bovine serum albumin (BSA) assay and a quartz crystal microbalance (QCM-D). Our findings revealed that the LC membrane of Masson pine adsorbed more BSA than that of poplar, indicating Masson pine LC molecules were more hydrophobic due to a higher proportion of guaiacyl (G)-type lignin units.

Interaction Mechanism between Bovine Serum Albumin and Polyethylene Glycol Revealed with Elastic Light Scattering Spectroscopy

2013 ◽  
Vol 704 ◽  
pp. 43-50
Author(s):  
Wen Zhi Zhang ◽  
Kuan Zhang ◽  
Jian Long Zheng ◽  
Hong Shu Chen ◽  
Wei Xing Chen ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Light Scattering ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Interaction Mechanism ◽  
Interaction Force ◽  
Elastic Light Scattering ◽  
Apparent Binding Constant ◽  
Light Scattering Spectroscopy

In order to gain deeper insight into the interaction mechanism between bovine serum albumin (BSA) and polyethylene glycol (PEG), the present work applied elastic light scattering (ELS) spectroscopy to investigate the interaction between BSA and PEG, and explore the effects of concentration and molecular weight of PEG on the interaction at physiological pH. The results showed that the interaction force existed between linear PEG and spherical BSA molecules was mainly hydrogen bonding. In addition, the apparent binding constant of system was evaluated by model calculation.

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