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Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A2 from Bothrops atrox snake venom

Overview of attention for article published in Journal of Venomous Animals and Toxins including Tropical Diseases, August 2015
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Title
Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A2 from Bothrops atrox snake venom
Published in
Journal of Venomous Animals and Toxins including Tropical Diseases, August 2015
DOI 10.1186/s40409-015-0027-6
Pubmed ID
Authors

Danilo L. Menaldo, Anna L. Jacob-Ferreira, Carolina P. Bernardes, Adélia C. O. Cintra, Suely V. Sampaio

Abstract

Snake venoms are complex mixtures of inorganic and organic components, mainly proteins and peptides. Standardization of methods for isolating bioactive molecules from snake venoms is extremely difficult due to the complex and highly variable composition of venoms, which can be influenced by factors such as age and geographic location of the specimen. Therefore, this study aimed to standardize a simple purification methodology for obtaining a P-I class metalloprotease (MP) and an acidic phospholipase A2 (PLA2) from Bothrops atrox venom, and biochemically characterize these molecules to enable future functional studies. To obtain the toxins of interest, a method has been standardized using consecutive isolation steps. The purity level of the molecules was confirmed by RP-HPLC and SDS-PAGE. The enzymes were characterized by determining their molecular masses, isoelectric points, specific functional activity and partial amino acid sequencing. The metalloprotease presented molecular mass of 22.9 kDa and pI 7.4, with hemorrhagic and fibrin(ogen)olytic activities, and its partial amino acid sequence revealed high similarity with other P-I class metalloproteases. These results suggest that the isolated metalloprotease is Batroxase, a P-I metalloprotease previously described by our research group. The phospholipase A2 showed molecular mass of 13.7 kDa and pI 6.5, with high phospholipase activity and similarity to other acidic PLA2s from snake venoms. These data suggest that the acidic PLA2 is a novel enzyme from B. atrox venom, being denominated BatroxPLA2. The present study successfully standardized a simple methodology to isolate the metalloprotease Batroxase and the acidic PLA2 BatroxPLA2 from the venom of B. atrox, consisting mainly of classical chromatographic processes. These two enzymes will be used in future studies to evaluate their effects on the complement system and the inflammatory process, in addition to the thrombolytic potential of the metalloprotease.

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Mendeley readers

The data shown below were compiled from readership statistics for 48 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 48 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 14 29%
Student > Master 8 17%
Student > Ph. D. Student 7 15%
Researcher 4 8%
Student > Doctoral Student 3 6%
Other 5 10%
Unknown 7 15%
Readers by discipline Count As %
Agricultural and Biological Sciences 14 29%
Biochemistry, Genetics and Molecular Biology 11 23%
Chemistry 6 13%
Immunology and Microbiology 3 6%
Engineering 2 4%
Other 4 8%
Unknown 8 17%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 August 2015.
All research outputs
#2,914,140
of 5,482,709 outputs
Outputs from Journal of Venomous Animals and Toxins including Tropical Diseases
#109
of 221 outputs
Outputs of similar age
#104,524
of 192,038 outputs
Outputs of similar age from Journal of Venomous Animals and Toxins including Tropical Diseases
#6
of 11 outputs
Altmetric has tracked 5,482,709 research outputs across all sources so far. This one is in the 33rd percentile – i.e., 33% of other outputs scored the same or lower than it.
So far Altmetric has tracked 221 research outputs from this source. They receive a mean Attention Score of 3.1. This one is in the 32nd percentile – i.e., 32% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 192,038 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 35th percentile – i.e., 35% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 11 others from the same source and published within six weeks on either side of this one. This one is in the 18th percentile – i.e., 18% of its contemporaries scored the same or lower than it.