Article

Recombinant hyaluronidase

Bascom Palmer Eye Institute, University of Miami, Miami, Florida, USA.
Clinical and Experimental Ophthalmology (Impact Factor: 1.95). 06/2013; 42(3). DOI: 10.1111/ceo.12154
Source: PubMed

ABSTRACT We read with interest the article by Zamora-Alejo and colleagues (1) . We laud them for presenting a series of delayed onset hyaluronidase-related complications, and alerting your readership of this potential hazard. Although we concur with their inference of hyaluronidase-induced tissue toxicity, we cogitate that these were type B adverse drug reactions (idiosyncratic) (2) .

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    ABSTRACT: Hyaluronidase catalyzes the hydrolysis of hyaluronan polymers to N-acetyl-D-glucosamine and D-glucuronic acid. This enzyme is a dimer of identical subunits. Hyaluronidase has different pharmaceutical and medical applications. Previously, we produced a recombinant hyaluronidase antigenic fragment of Streptococcus pyogenes. This study aimed to improve the protein production and purity of hyaluronidase recombinant protein from S. pyogenes. In addition, the enzymatic activity of this protein was investigated. The expression of hyaluronidase antigenic fragments was optimized using IPTG concentration, time of induction, temperature, culture, and absorbance of 0.6-0.8-1 at 600 nm. Afterwards, the expressed proteins were purified and the enzymatic activity was assessed by turbid metric method. Data indicated that maximum protein is produced in OD = 0.8, 0.5 mM Isopropyl β-D-1-thiogalactopyranoside (IPTG), 37ºC, NB 1.5x, without glucose, incubated for overnight. The enzymatic activity of the recombinant protein was similar to the commercial form of hyaluronidase. The results showed that an antigenic fragment of the recombinant hyaluronidase protein from S. pyogenes has a considerable enzymatic activity. It can be suggested to use it for medical purposes. In addition, applications of bioinformatics software would facilitate the production of a smaller protein with same antigenic properties and enzymatic activity.
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