Search results
Results From The WOW.Com Content Network
The emperor scorpion (Pandinus imperator) is one of the largest species of scorpion in the world, with adults averaging about 20 centimetres (7.9 in) in length and a weight of 30 g. [2] However, some species of forest scorpions are fairly similar to the emperor scorpion in size, and one scorpion, Heterometrus swammerdami , holds the record for ...
Pandinus is a genus of large scorpions belonging to the family Scorpionidae. It contains one of the most popular pet scorpions, the emperor scorpion (P. imperator). The genus is distributed across tropical Africa. [1] [2] [3]
Arizona bark scorpions do burrow, and are commonly found in homes, requiring only 1/16 of an inch for entry. [6] Arizona bark scorpions prefer riparian areas with mesquite, cottonwood, and sycamore groves, all of which have sufficient moisture and humidity to support insects and other prey species. The popularity of irrigated lawns, and other ...
Heterometrus longimanus, the Asian forest scorpion, is a species of scorpions belonging to the family Scorpionidae. [1] Description
The deathstalker is one of the most dangerous species of scorpions. [10] [11] Its venom is a powerful mixture of neurotoxins, with a low lethal dose. [12]While a sting from this scorpion is extraordinarily painful, it normally would not kill a healthy adult human.
This page was last edited on 21 December 2015, at 08:51 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.
Pi5 is a peptide that is purified from the venom of the African scorpion Pandinus imperator. [1] Pi in Pi5 is short for the 5th identified peptide of the scorpion Pandinus imperator. [1] As of July 2017, a total of 7 peptides purified from the venom of this scorpion have been characterized (Pi1-7). [1]
PiTX-Kα and PiTX-Kβ are 35-residue peptides, which are found to have an α-helix from residues 10 to 21 and two β-sheets (β 1 is from residues 26-28, β 2 is from residues 33-35). One face of the α-helix is anchored to the β-sheet by three disulfide bonds which are conserved in all members of the charybdotoxin family (R-K toxins). [ 1 ]