ArticleThe protein journal2019
Variation in the Protein Composition and Biological Activity of King Cobra (Ophiophagus hannah) Venoms.
Article in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides.Marine drugs · 2024Article
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- A novel angiotensin-I-converting enzyme inhibitory peptide from oyster: Simulated gastro-intestinal digestion, molecular docking, inhibition kinetics and antihypertensive effects in rats.Frontiers in nutrition · 2022Article
- King Cobra and snakebite envenomation: on the natural history, human-snake relationship and medical importance ofThe journal of venomous animals and toxins including tropical diseases · 2021Review
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- Two novel ACE inhibitory peptides isolated from longan seeds: purification, inhibitory kinetics and mechanisms.RSC advances · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biochemical properties and biological activities of the venom from three individual Ophiophagus hannah (King cobra) specimens was compared. The toxicity against mice, the cytotoxicity against five cell lines, and the antioxidant activity were measured. The KV2 venom showed a higher cytotoxicity than the KV6 and the non-cytotoxic KV9 venoms. Comparative analysis of the O. hannah venom proteins was performed after 2-dimensional (2-D) denaturing gel electrophoresis and reverse phase high performance liquid chromatography (RP-HPLC). 2-D analysis by isoelectric focusing (IEF) Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) resolution of the venoms revealed significant differences between all three venoms, with most spots being unique to that venom. Only 2 out of the 13-16 distinct spots were common to all three venoms, and four spots were common to KV6 and KV9. KV2 had the highest proportion of low molecular mass spots, and KV6 and KV9 appeared more related to each other than to KV9. From peptide mass mapping by matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) and MASCOT-based amino acid sequence database searching, the two venom proteins that were common to all three specimens are likely to be ophanin and acidic phospholipase A
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Registered trials
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