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Literature summary for 3.2.1.35 extracted from

  • Xin, Y.; Hao, M.; Fan, G.; Zhang, Y.; Zheng, M.; Zhang, L.
    Affinity adsorption of bovine hyaluronidase with ligands targeting to active site (2018), J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 1092, 422-431 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-aminobenzimidazole 0.04 mM, 92% inhibition Bos taurus
6-chloromethyluracil 0.05 mM, 94% inhibition Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus Q5E985
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-

Purification (Commentary)

Purification (Comment) Organism
according to their inhibition activity for hyaluronidases, 6-chloromethyluracil and 2-aminobenzimidazole are coupled with sepharose beads for the affinity adsorption of bovine hyaluronidase-1. In good accordance with structural simulation, the ligands designed from 2-aminobenzimidazole show much higher specificity for the target enzyme, because they had more H bonds and pi-pi interactions with target sites. After optimization, through one step of affinity adsorption with sorbent L-4, bovine hyaluronidase can be isolated from the supernatant of bovine testes extract, with purity and recovery up to 96.4% and 89.4%, respectively. Based on the less steps of purification, short time consuming, higher purity, and higher activity recoveries, industrial application of this method is of great potential Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
testis
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Bos taurus
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Synonyms

Synonyms Comment Organism
hyaluronidase-1
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Bos taurus