1984
DOI: 10.1016/0305-0491(84)90170-6
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Acid proteinase activity in fish II. Purification and characterization of cathepsins B and D from Mujil auratus muscle

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Cited by 16 publications
(12 citation statements)
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“…The activity in cut off from saithe increased after 10 min at 30 1C and liver from cod showed increased activity after 10 min at 50 1C. Other researchers have also found that pre-incubation at temperatures from 30 to 50 1C led to activation of cathepsins (Bonete et al, 1984b;Porter, Koury, & Stone, 1996). This activation is most likely due to activation of pro-cathepsins or dissociation of inhibitor complexes (Porter et al, 1996).…”
Section: Heat Stabilitymentioning
confidence: 82%
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“…The activity in cut off from saithe increased after 10 min at 30 1C and liver from cod showed increased activity after 10 min at 50 1C. Other researchers have also found that pre-incubation at temperatures from 30 to 50 1C led to activation of cathepsins (Bonete et al, 1984b;Porter, Koury, & Stone, 1996). This activation is most likely due to activation of pro-cathepsins or dissociation of inhibitor complexes (Porter et al, 1996).…”
Section: Heat Stabilitymentioning
confidence: 82%
“…The activation energy of cathepsin B was significantly lower in cut off compared to viscera and liver, indicating that cathepsin B in cut off was less sensitive to temperature than in the two other fractions. The activation energy in cut off was also lower than that found for cathepsin B from the Mujil auratus muscle, 44.4 kJ/mol (Bonete et al, 1984b).…”
Section: Article In Pressmentioning
confidence: 96%
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“…6). Activation of proteolytic enzymes after pre-incubation at temperatures from 30 to 50 1C have been reported (Bonete, Manjon, Llorca, & Iborra, 1984b;Porter, Koury, & Stone, 1996), and is most likely due to activation of pro-enzymes or dissociation of inhibitor complexes. After 10 min at 50 1C the activity at pH 5 and 7 was reduced to 2675% and 3070.1% of initial activity, respectively, and after 10 min at 70 1C, activities were less than 2.5%.…”
Section: Heat Stabilitymentioning
confidence: 97%
“…CatB protein has been purified from several types of fish, but most purified protein only contains the heavy chain (Bonete and others ; Matsumiya and others ; Sherekar and others ) or segment (Tan and others ) of this protease. However, more comprehensive information about CatB structural features and chemical nature can be obtained by the research of gene cloning and recombinant expression.…”
Section: Resultsmentioning
confidence: 99%