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vriesea friburgensis/cysteine
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De novo assembly of Vriesea carinata leaf transcriptome to identify candidate cysteine-proteases.
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Vriesea carinata is an endemic bromeliad from the Brazilian Atlantic Forest. It has trichome and tank system in their leaves which allows to absorb water and nutrients. It belongs to Bromeliaceae family, which includes several species highly enriched of cysteine-proteases (CysPs). These proteolytic
Four Ca2+-dependent proteinase activities isolated from crustacean muscle differ in size, net charge, and sensitivity to Ca2+ and inhibitors.
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Four Ca2+-dependent proteinase activities in lobster claw and abdominal muscle have been resolved by high-performance liquid chromatography on gel filtration and ion-exchange columns. These activities, which do not appear to be generated by autolytic or other degradative processes, differed from
Purification and characterization of a multicatalytic proteinase from crustacean muscle: comparison of latent and heat-activated forms.
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A high-molecular-weight (Mr 740,000) multicatalytic proteinase (MCP) was purified over 3100-fold from soluble extracts of lobster claw and abdominal muscles. The enzyme was extracted from muscle in a latent state; brief (3 min) heating of an ammonium sulfate fraction (45-65% saturation) at 60
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