Current Issues of Pharmacy and Medical Sciences

Antihypertensive and anticoagulant properties of glycosaminoglycans extracted from the sturgeon (Acipenser persicus) cartilage

Curr Issues Pharm Med Sci., Vol. 31, No. 4, 163-169

Katayoon Karimzadeh

Department of Marine Biology, Lahijan Branch, Islamic Azad University, Lahijan, Iran


DOI 10.1515/cipms-2018-0031

© 2018 Author(s). This is an open access article distributed under the Creative Commons Attribution-NonComercial-No Derivs licence (http://creativecommons.org/licenses/by-nc-nd/3.0/)

Abstract

Large amounts of valuable waste are produced during sea food processing. This has a great potential for conversion to biologically active proteins and polysaccharides. Among these compounds, sulfated polysaccharides have been considered due to their many biological properties.
The present work was conducted to study anticoagulant activities and angiotensin-I converting enzyme (ACE) inhibitory effects of glycosaminoglycans (GAGs) extracted from the cartilage of sturgeon (Acipenser persicus). The enzymatic extraction of sturgeon cartilage was performed in the presence of cetylpyridinium chloride salt. The structure was characterized via electron microscope and Fourier transform infrared spectroscopy (FTIR) analysis. Herein, ACE inhibitory and anticoagulant properties of extracted GAGs were determined.
The amount of GAGs was 6.8±1.3% of cartilage dry weight. GAGs showed good activity in ACE inhibitory – with a highest level of 85.7%. The derived anticoagulant activity indexes, APPT (activated partial thromboplastin time) and TT (Thrombin time) of the extracted polysaccharide showed a prolonging of clotting time, compare to control. The results of this study revealed that the cartilage extracted GAGs possess promising ACE inhibitory properties and anticoagulant effects. Thus, the product can be substituted for blood reducing drugs and antithrombotic agents at least in laboratory conditions.

 

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Keywords

sturgeon, cartilage, angiotensin I-converting enzyme, anticoagulant activity, alcalase.

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