Primary structures of the N-linked carbohydrate chains from honeybee venom phospholipase A2
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چکیده
منابع مشابه
Therapeutic application of natural inhibitors against snake venom phospholipase A2
Natural inhibitors occupy an important place in the potential to neutralize the toxic effects caused by snake venom proteins and enzymes. It has been well recognized for several years that animal sera, some of the plant and marine extracts are the most potent in neutralizing snake venom phospholipase A(2) (svPLA(2)). The implication of this review to update the latest research work which has be...
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As polyphenolic compounds isolated from plants extracts, flavonoids have been applied to various pharmaceutical uses in recent decades due to their anti-inflammatory, cancer preventive, and cardiovascular protective activities. In this study, we evaluated the effects of the flavonoid quercetin on Crotalus durissus terrificus secretory phospholipase A2 (sPLA2), an important protein involved in t...
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(3-Bungarotoxin ((3-BuTX) induces twitching of innervated frog muscle and subsequently blocks transm itter release from motor nerve endings. These actions of P-BuTX are prevented if the nerve-muscle junctions are pretreated with a low concentration of phospholipase A2 from bee venom. When the Ca2+ in the external fluid is replaced by Sr2+, the phospho lipase activity of P-BuTX is negligible an...
متن کاملCrystal structure of bee-venom phospholipase A2: correction.
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متن کاملStructure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus.
An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a d...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1993
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1993.tb17870.x