All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10191762" target="_blank" >RIV/00216208:11310/14:10191762 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/14:00428463

  • Result on the web

    <a href="http://dx.doi.org/10.1016/j.pep.2013.12.005" target="_blank" >http://dx.doi.org/10.1016/j.pep.2013.12.005</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.pep.2013.12.005" target="_blank" >10.1016/j.pep.2013.12.005</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis

  • Original language description

    Carnivorous plants of the genus Nepenthes produce their own aspartic proteases, nepenthesins, to digest prey trapped in their pitchers. Nepenthesins differ significantly in sequence from other aspartic proteases in the animal or even plant kingdoms. Thisdifference, which also brings more cysteine residues into the structure of these proteases, can be a cause of uniquely high temperature and pH stabilities of nepenthesins. Their detailed structure characterization, however, has not previously been possible due to low amounts of protease present in the pitcher fluid and also due to limited accessibility of Nepenthes plants. In the present study we describe a convenient way for obtaining high amounts of nepenthesin-1 from Nepenthes gracilis using heterologous production in Escherichia coli. The protein can be easily refolded in vitro and its characteristics are very close to those described for a natural enzyme isolated from the pitcher fluid. Similarly to the natural enzyme, recombinant

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2014

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Protein Expression and Purification

  • ISSN

    1046-5928

  • e-ISSN

  • Volume of the periodical

    95

  • Issue of the periodical within the volume

    March 2014

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    8

  • Pages from-to

    121-128

  • UT code for WoS article

    000332192900017

  • EID of the result in the Scopus database