[Isolation and purification of proteolytic enzymes on organo-silica sorbents with immobilized gramicidin S].
Abstract: Biospecific sorbents for affinity chromatography of proteolytic enzymes have been synthesized by attaching cyclopeptide antibiotic gramicidin S to organo-silica supports. It is shown possible to attach gramicidin S to the organo-silica supports using glutaric aldehyde, p-benzoquinone, soluble and insoluble carbodiimides. The sorbents prepared by these methods were successfully applied for the purification of the crude pepsin from horse gastric juice and proteolytic complex produced by Acremonium chrysogenum.
Publication Date: 1987-11-01 PubMed ID: 2448932 The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- English Abstract
- Journal Article
Summary
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This research involves the development of biospecific sorbents for purification of proteolytic enzymes using the antibiotic gramicidin S attached to organo-silica supports, which has been successfully tested with the purification of pepsin from horse gastric juice and a proteolytic complex produced by a type of fungus.
Understanding Biospecific Sorbents
- Biospecific sorbents are substances that can attract and hold specific molecules and help in their separation from a mixture. In this research, these sorbents are used in the process of affinity chromatography, a method used to separate and purify specific molecules from a mixture.
Role of Gramicidin S
- Gramicidin S is a cyclopeptide antibiotic. In this research, it’s used as the specific molecule to attach to organo-silica supports and create the biospecific sorbents.
Attachment Process
- The process of attaching gramicidin S to the organo-silica supports involves the use of certain agents namely glutaric aldehyde, p-benzoquinone, soluble and insoluble carbodiimides. These agents help in forming a strong bond between gramicidin S and organo-silica supports.
Testing and Application of the Biospecific Sorbents
- The effective and successful application of these biospecific sorbents was evaluated by purifying the crude pepsin from horse gastric juice and proteolytic complex produced by Acremonium chrysogenum. Pepsin is a type of proteolytic enzyme that helps in the digestion of proteins. The proteolytic complex produced by Acremonium chrysogenum implies a group of proteolytic enzymes produced by this fungus.
- The successful purification indicates that the sorbents created in this research can be utilized for the purification of similar proteolytic enzymes.
Cite This Article
APA
Ignatchenko AP, Bogomaz VI, Tugaĭ VA, Chuĭko AA.
(1987).
[Isolation and purification of proteolytic enzymes on organo-silica sorbents with immobilized gramicidin S].
Ukr Biokhim Zh (1978), 59(6), 28-33.
Publication
Researcher Affiliations
MeSH Terms
- Animals
- Chromatography, Affinity
- Gramicidin
- Horses
- Peptide Hydrolases / isolation & purification
- Silicon
Citations
This article has been cited 1 times.- Weetall HH. Preparation of immobilized proteins covalently coupled through silane coupling agents to inorganic supports. Appl Biochem Biotechnol 1993 Jun;41(3):157-88.
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