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Purification of 57kDa Hyaluronidase from the venom of Conus betulinus (Linnaeus, 1758)
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Abstract
The enzyme hyaluronidase cleaves the substrate hyaluronic acid. In the study, hyaluronidase was isolated from the venom gland of C. betulinus and characterised using SDS-PAGE, FTIR, and HPLC. The protein content of crude venom is approximately 4mg/ml, whereas purification with Sepacryl S-100 yielded 0.04mg/ml protein with 0.463TRU/mg specific activity. The detected hyaluronidase had a molecular weight of 57kDa when compared to a standard protein marker. The presence of a peak at Rt 57.23 as hyaluronidase is revealed by HPLC analysis, and the wavelength pattern is similar to the standard bovine testicular hyaluronidase.
Title: Purification of 57kDa Hyaluronidase from the venom of Conus betulinus (Linnaeus, 1758)
Description:
Abstract
The enzyme hyaluronidase cleaves the substrate hyaluronic acid.
In the study, hyaluronidase was isolated from the venom gland of C.
betulinus and characterised using SDS-PAGE, FTIR, and HPLC.
The protein content of crude venom is approximately 4mg/ml, whereas purification with Sepacryl S-100 yielded 0.
04mg/ml protein with 0.
463TRU/mg specific activity.
The detected hyaluronidase had a molecular weight of 57kDa when compared to a standard protein marker.
The presence of a peak at Rt 57.
23 as hyaluronidase is revealed by HPLC analysis, and the wavelength pattern is similar to the standard bovine testicular hyaluronidase.
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