نتایج جستجو برای: aspartic protease

تعداد نتایج: 68868  

2016
Ina Coburger Yvonne Schaub Dirk Roeser Kornelia Hardes Patrick Maeder Nina Klee Torsten Steinmetzer Diana Imhof Wibke E. Diederich Manuel E. Than

GxGD-type intramembrane cleaving proteases (I-CLiPs) form a family of proteolytic enzymes that feature an aspartate-based catalytic mechanism. Yet, they structurally and functionally largely differ from the classical pepsin-like aspartic proteases. Among them are the archaeal enzyme FlaK, processing its substrate FlaB2 during the formation of flagella and γ-secretase, which is centrally involve...

Journal: :The Journal of biological chemistry 1994
S Norioka S Ohta T Ohara S I Lim F Sakiyama

Achromobacter protease I is a lysine-specific serine protease that Achromobacter lyticus M497-1 extracellularly secretes. The structural aspects necessary for the protease to function were investigated by means of site-directed mutagenesis to identify the constituents of the catalytic triad and the amino acid residue responsible for lysine specificity. The precursor molecules, which were produc...

Journal: :Plant physiology 1996
P. C. Bethke S. Hillmer R. L. Jones

Within the cereal aleurone reserve proteins are stored in specialized organelles, the protein storage vacuoles (PSV). We developed an aqueous method for the isolation of intact PSV. Barley (Hordeum vulgare L. cv Himalaya) aleurone protoplasts were gently lysed by passing them through a syringe needle. PSV were separated from cytoplasmic components by microfiltration and low-speed centrifugation...

2002
Paul C. Bethke Stefan Hillmer

Within the cereal aleurone reserve proteins are stored in specialized organelles, the protein storage vacuoles (PSV). W e developed an aqueous method for the isolation of intact PSV. Barley (Hordeum vulgare 1. cv Himalaya) aleurone protoplasts were gently lysed by passing them through a syringe needle. PSV were separated from cytoplasmic components by microfiltration and low-speed centrifugatio...

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