Purification and characterization of an intracellular aspartyl acid proteinase (pumAi) from Ustilago maydis

$50.00 plus tax (Refund Policy)

Buy Article:

Abstract:

The intracellular proteinase pumAi in Ustilago maydis has been associated with yeast-mycelium dimorphic transition. The proteinase was purified from a cell-free extract by ammonium sulfate fractionation and chromatographic steps including hydrophobic interactions on a Phenyl Superose column, ion exchange on a Mono Q column, and gel filtration on Superose 12 columns. The enzyme has a mass of 35.3–36.6 kDa, a pH and temperature optimum of 4.0 and 40 °C, respectively, and a pI of 5.5. The enzyme degraded hemoglobin, gelatin, albumin, and casein, but not collagen, and the enzymatic activity was strongly inhibited by pepstatin A, an aspartyl proteinase-specific inhibitor. The biochemical characteristics of pumAi are similar to other fungal intracellular aspartyl proteinases, however, this is the first biochemical characterization of a basidiomycete proteinase probably associated with dimorphic yeast-mycelium transition.Key words: aspartyl proteinase, yeast-mycelium transition, Ustilago maydis.

La protéinase intracellulaire pumAi de Ustilago maydis a été associée à la transition dimorphique de levûre au mycélium. L'enzyme a été purifiée à partir d'un extrait exempt de cellules par une précipitation au sulfate d'ammonium, suivie d'une chromatographie d'interaction hydrophobe sur phenyl-superose, une chromatographie d'interéchange sur Mono Q et une filtration sur Superose 12. Cette enzyme a une masse évaluée à 35.3–36.6 kDa, un pH et une température optimums dénviron 4.0 et 40 °C, respectivement, et un pI de 5.5. L'enzyme hydrolyses hémoglobine, gélatine, albumine et caséine mais no collagène, et l'activité enzymatique était fortement inhibée en présence de pepstatin A, un inhibitor spécifique de aspartique protéases. Les caractéristiques biochimiques de pumAi sont semblable à autre aspartique protéinases intracellulaires de champignons, nonobstant ce es le premier caractérisation biochimie de une protéinase de basidiomycète peut être associée à la transition dimorphique de levûre au mycélium.Mots clés : protéinase aspartique, dimorphique de levûre au micelium, Ustilago maydis.

Document Type: Research Article

Publication date: February 1, 2005

More about this publication?
  • Published since 1954, this monthly journal contains new research in the field of microbiology including applied microbiology and biotechnology; microbial structure and function; fungi and other eucaryotic protists; infection and immunity; microbial ecology; physiology, metabolism and enzymology; and virology, genetics, and molecular biology. It also publishes review articles and notes on an occasional basis, contributed by recognized scientists worldwide.
  • Information for Authors
  • Submit a Paper
  • Subscribe to this Title
  • Terms & Conditions
  • Sample Issue
  • Reprints & Permissions
  • ingentaconnect is not responsible for the content or availability of external websites

Tools

Favourites

Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
X
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more