Purification and characterization of a novel C-type hemolytic lectin for clot lysis from the fresh water clam Villorita cyprinoides: A possible natural thrombolytic agent against myocardial infarction |
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| Institution: | 1. International Centre for Nanobiotechnology (ICN), CMST Campus, Manonmaniam Sundaranar University, Rajakkamanagalam, Kanyakumari Dist., 629502 TN, India;2. Xpression Biotek (Pvt) Ltd., Marthandam, Kanyakumari Dist., TN, India;1. AGH University of Science and Technology, Faculty of Metals Engineering and Industrial Computer Science, Al. A. Mickiewicza 30, 30-059 Kraków, Poland;2. Pedagogical University of Cracow, Institute of Technology, ul. Podchorążych 2, 30-084 Kraków, Poland;1. Programa de Pós-Graduação em Ciências Fisiológicas, Fisiologia Animal Comparada, Universidade Federal do Rio Grande—FURG, Avenida Itália, Km 8, CEP 96201-900 Rio Grande, RS, Brazil;2. Programa de Pós-Graduação em Aquicultura, Universidade Federal do Rio Grande—FURG, Avenida Itália, Km 8, CEP 96201-900 Rio Grande, RS, Brazil;3. Instituto de Ciências Biológicas, Universidade Federal do Rio Grande—FURG, Avenida Itália, Km 8, CEP 96201-900 Rio Grande, RS, Brazil;4. Instituto de Oceanografia, Universidade Federal do Rio Grande—FURG, Avenida Itália, Km 8, CEP 96201-900 Rio Grande, RS, Brazil;1. Department of Marine Biology and Aquaculture, College of Marine Science, Gyeongsang National University, 38 Cheondaegukchi-Gil, Tongyeong, Gyeongnam 650-160, Republic of Korea;2. School of Biotechnology, Yeungnam University, Gyeongsan, Gyeongbuk 712-749, Republic of Korea;3. Pathology Division, National Fisheries Research and Development Institute, Busan 619-900, Republic of Korea;4. Oil & POPs Research Group, Korea Institute of Ocean Science & Technology, 391 Jangbuk-Ri, Jangmok-Myon, Geoje 656-834, Republic of Korea;1. Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12, Zhongguancun South Street, Beijing 100081, PR China;2. National Animal Husbandry Extension Service, Beijing 100125, PR China |
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| Abstract: | Villorita cyprinoides (black clam) is a fresh water clam that belongs as a bivalve to the group of mollusc. The saline extracts from the muscle reveal high titers of agglutination potency on trypsin-treated rabbit erythrocytes. With the help of affinity chromatography a hemolytic protein with lectin activity which could all be inhibited by d-galactose were isolated. The lectins were separated on DEAE-cellulose and the main component was purified after an additional step of gel filtration on sephadex G-75. The main component is a non-glycosylated protein with a molecular weight of 96,560 Da determined by MALDI-ToF, consisting of a single protein chain and characterized by the lack of polymers and intermediate disulfide bonds. The pure main lectin with clot lytic feature shows two bands at molecular weights 36,360 and 26, 520 Da. Optimal inhibition of the pure lectin is achieved by d-galactose containing oligo- and polysaccharides. The lectin activity decreased above 40 °C and was lost at 62 °C, the stability over the pH range between 7.0 and 8.0 and requires divalent cations for their activity. The novel C-type hemolytic lectin for clot lysis from the clam Villorita cyprinoides was identified and evaluated, the purified hemolytic lectin (0.35 mg/ml and 0.175 mg/ml) enhanced clot lysis activity when compared to the different concentration (5 mg/ml and 1 mg/ml) of commercial streptokinase. In the present study identified hemolytic lectin was a rapid and effective clot lytic molecule and could be developed as new drug molecule in future. |
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| Keywords: | Clam Clot lysis Streptokinase Hemolytic lectin MALDI-ToF |
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