↓ Skip to main content

Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

Overview of attention for article published in Journal of Venomous Animals and Toxins including Tropical Diseases, August 2015
Altmetric Badge

About this Attention Score

  • Average Attention Score compared to outputs of the same age

Mentioned by

twitter
1 tweeter
facebook
1 Facebook page

Citations

dimensions_citation
24 Dimensions

Readers on

mendeley
145 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability
Published in
Journal of Venomous Animals and Toxins including Tropical Diseases, August 2015
DOI 10.1186/s40409-015-0025-8
Pubmed ID
Authors

Karla C. F. Bordon, Gisele A. Wiezel, Hamilton Cabral, Eliane C. Arantes

Abstract

Crotalus durissus terrificus venom (CdtV) is one of the most studied snake venoms in Brazil. Despite presenting several well known proteins, its L-amino acid oxidase (LAAO) has not been studied previously. This study aimed to isolate, characterize and evaluate the enzyme stability of bordonein-L, an LAAO from CdtV. The enzyme was isolated through cation exchange, gel filtration and affinity chromatography, followed by a reversed-phase fast protein liquid chromatography to confirm its purity. Subsequently, its N-terminal amino acid sequence was determined by Edman degradation. The enzyme activity and stability were evaluated by a microplate colorimetric assay and the molecular mass was estimated by SDS-PAGE using periodic acid-Schiff staining and determined by mass spectrometry. The first 39 N-terminal amino acid residues exhibited high identity with other snake venom L-amino acid oxidases. Bordonein-L is a homodimer glycoprotein of approximately 101 kDa evaluated by gel filtration. Its monomer presents around 53 kDa estimated by SDS-PAGE and 58,702 Da determined by MALDI-TOF mass spectrometry. The enzyme exhibited maximum activity at pH 7.0 and lost about 50 % of its activity after five days of storage at 4 °C. Bordonein-L's activity was higher than the control when stored in 2.8 % mannitol or 8.5 % sucrose. This research is pioneering in its isolation, characterization and enzyme stability evaluation of an LAAO from CdtV, denominated bordonein-L. These results are important because they increase the knowledge about stabilization of LAAOs, aiming to increase their shelf life. Since the maintenance of enzymatic activity after long periods of storage is essential to enable their biotechnological use as well as their functional studies.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 145 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Brazil 1 <1%
Unknown 144 99%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 8 6%
Student > Ph. D. Student 7 5%
Researcher 6 4%
Student > Master 5 3%
Student > Doctoral Student 3 2%
Other 7 5%
Unknown 109 75%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 11 8%
Agricultural and Biological Sciences 9 6%
Medicine and Dentistry 4 3%
Nursing and Health Professions 3 2%
Materials Science 2 1%
Other 7 5%
Unknown 109 75%

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 01 September 2015.
All research outputs
#9,618,589
of 12,526,623 outputs
Outputs from Journal of Venomous Animals and Toxins including Tropical Diseases
#221
of 321 outputs
Outputs of similar age
#150,086
of 238,842 outputs
Outputs of similar age from Journal of Venomous Animals and Toxins including Tropical Diseases
#2
of 3 outputs
Altmetric has tracked 12,526,623 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 321 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 15th percentile – i.e., 15% 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 238,842 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 31st percentile – i.e., 31% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 3 others from the same source and published within six weeks on either side of this one.