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1.
J Oleo Sci ; 70(3): 439-451, 2021 Mar 04.
Article in English | MEDLINE | ID: mdl-33583922

ABSTRACT

This experiment treated perilla seeds with different concentrations of NaCl solution to enrich and purify their rosmarinic acid (RosA). The results showed that low concentrations of salt (0-20 mmol/L) promoted seed germination, while high concentrations (> 20 mmol/L) inhibited germination. When the salt concentration was 20 mmol/L, the germination rate was the highest. The content of RosA in germinated perilla seeds was 3.5 mg/g, which was 3.5 times as much as that in the seeds without germination. The RosA was purified using NK-109 macroporous resin and its adsorption kinetics, isotherms and thermodynamics were determined. The adsorption kinetics showed that the adsorption behavior of RosA in NK-109 resin conformed to the pseudo-second-order kinetic model. The model for RosA in the NK-109 resin exhibited Langmuir adsorption based on a spontaneous exothermic process according to its adsorption thermodynamics, which included both physical and chemical adsorption. The optimized process conditions were as follows: the loading concentration of 0.04 mg/mL, loading volume of 40 mL, 70% methanol as the eluent with the volume of 60 mL, and the purity of RosA was 42.1%.


Subject(s)
Benzophenanthridines , Cinnamates/chemistry , Cinnamates/isolation & purification , Depsides/chemistry , Depsides/isolation & purification , Thermodynamics , Adsorption , Dose-Response Relationship, Drug , Germination/drug effects , Methanol , Perilla/chemistry , Pharmacokinetics , Porosity , Seeds/chemistry , Seeds/physiology , Sodium Chloride/pharmacology , Solutions , Rosmarinic Acid
2.
Protein & Cell ; (12): 569-572, 2013.
Article in English | WPRIM (Western Pacific) | ID: wpr-757774

ABSTRACT

Ig superfamily (IgSF) constitutes the largest superfamily in human genome. In particular, Ig-like domains are the most abundant structural module within cell surface receptors, functioning in nervous as well as immune system. Here I describe some key sequence signature of an I-set Ig-like domain from known structures of IgSF members. These signature residues define the I-set Ig-like domain, which should aid structural and functional studies of cell surface receptors.


Subject(s)
Humans , Amino Acid Sequence , Hydrogen Bonding , Immunoglobulins , Chemistry , Metabolism , Molecular Sequence Data , Protein Folding , Protein Structure, Tertiary
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