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1.
Electron. j. biotechnol ; 8(1): 09-16, Apr. 2005. ilus
Article in English | LILACS | ID: lil-448777

ABSTRACT

Biotechnology education in developing nations remains one of the rate limiting factors in achieving optimal human resource capacity to drive and tap the bio-resources of these nations. Many developing countries are situated within rich bio-diversity enclaves. Biotechnology offers the promise of tapping these bio resources towards due process of developing these nations. While there may be a steady stream of biology and biotechnology based graduates, from Malaysian as well as foreign universities contributing to the human resource base for these countries, the numbers and knowledge diversity produced, still lack the capacity to optimally power research and development as well as supply the industrial biotechnology sectors of these countries. Realizing the need to address these issues at the grassroots level of higher education, Malaysia has taken an active step of bringing biotechnology into the classrooms of high schools throughout the country. These future generations of Malaysians, are hoped to progress towards manning and driving Malaysia's BioValley initiatives (a biotech based R&D and industry cluster), towards the national dream of developed nation status by the year 2020, using biotechnology as an economic growth vehicle. Here, we share our experiences in developing and proliferating a biotechnology awareness program for Malaysian high schools. It is hoped that similar programs will strive towards similar objectives in other developing countries.


Subject(s)
Biotechnology/education , Schools, Medical , Awareness , Developing Countries , Malaysia
2.
Int J Biochem ; 21(12): 1421-6, 1989.
Article in English | MEDLINE | ID: mdl-2612728

ABSTRACT

1. The major phospholipase A2 (PLA-DE4) of the venom of Trimeresurus purpureomaculatus (shore pit viper) has been purified to electrophoretic homogeneity. 2. The isoelectric point of the purified enzyme was determined to be 4.20, and the mol. wt was 31,700 as estimated by Sephadex G-75 gel filtration chromatography; and 14,000 as estimated by SDS-polyacrylamide gel electrophoresis. The purified enzyme hydrolyzed phosphatidylcholine (PC) faster than phosphatidylethanolamine (PE), whereas phosphatidylserine (PS) was not hydrolyzed at all (PC greater than PE greater than PS =0). However, in reaction system consisted of mixtures of PC and PS, phosphatidylserine was effectively hydrolyzed by the enzyme. 4. The phospholipase A2 exhibited edema-forming activity but not hemolytic, hemorrhagic or anticoagulant activities. It was not lethal to mice at a dosage of 10 micrograms/g by i.v. route.


Subject(s)
Crotalid Venoms/analysis , Phospholipases A/isolation & purification , Phospholipases/isolation & purification , Acetophenones , Amino Acids/analysis , Animals , Blood Coagulation/drug effects , Chromatography, DEAE-Cellulose , Chromatography, Gel , Crotalid Venoms/toxicity , Edema/chemically induced , Electrophoresis, Polyacrylamide Gel , Guinea Pigs , Hemolysis/drug effects , Hemorrhage/chemically induced , In Vitro Techniques , Isoelectric Focusing , Mice , Molecular Weight , Phospholipases A/metabolism , Phospholipases A/toxicity , Phospholipases A2 , Rabbits , Substrate Specificity
3.
Toxicon ; 26(11): 989-96, 1988.
Article in English | MEDLINE | ID: mdl-3245058

ABSTRACT

The toxic and biological activities of four samples of Trimeresurus purpureomaculatus venom were examined. The lethality, protein composition and biological activities of the four venom samples were similar. Three of the venom samples had LD50 (i.v.) values of 0.9 micrograms/g while the fourth had a lower LD50 (i.v.) of 0.45 micrograms/g. All four venom samples exhibited hemorrhagic, edema-inducing, anticoagulant and thrombin-like activities as well as the usual enzymes found in crotalid venoms. DEAE-Sephacel ion exchange chromatographic fractionation of the venom yielded 10 protein fractions. Only two fractions (fractions A and F) were lethal to mice; the major lethal fraction being fraction F. This fraction had an LD50 (i.v.) of 0.2 micrograms/g and exhibited hemorrhagic, edema-inducing and thrombin-like activity. It also exhibited phospholipase A, arginine ester hydrolase, arginine amidase, protease, 5'-nucleotidase, acetylcholinesterase and alkaline phosphomonoesterase activities. The lethal potency of fraction F is potentiated by fraction G, which exhibited anticoagulant activity as well as hemorrhagic, edema-inducing and enzymatic activities. Fractions F plus G account for almost 100% of the lethal potency of the venom.


Subject(s)
Crotalid Venoms/pharmacology , Animals , Chromatography, Ion Exchange , Crotalid Venoms/metabolism , Edema/chemically induced , Hemorrhage/chemically induced , Lethal Dose 50 , Mice
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