Cistein proteinases in the Boophilus microplus ovary
2003 - Volume: 43 Issue: 3 pages: 239-247
In this study on the acid proteolytic activity in the ovary of Boophilus microplus vitellogenic females, the inhibition assays showed the predominance of cysteine proteinase activity. Due to substrate specificity and pH dependency, cysteine proteinase activity appeared to be represented by cathepsin L-like and B-like activities, the first one with four days after oviposition reaching a maximum at day 2. The total ovary protein at this period developed a similar kinetic suggesting an association between cysteine proteinases and egg protein formation. The cathepsin L-like activity showed a significant increase with repletion due to the presence of a new active fraction (CPL), obtained from an anion exchange chromatography suggesting its closer relationship with vitellogenesis. CPL was activated at acid pH with a decrease in its molecular mass (275 kDa to 40-50 kDa), determined by gel filatration chromatography.
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