leupeptin การใช้

• Tissue samples are lysed in buffer supplemented with leupeptin to maintain enzymatic activity.
• Leupeptin is an organic compound produced by actinomycetes, which inhibits cysteine and threonine proteases.
• Alt = Crystal structure of Leupeptin ( silver ) in the Trypsin ( green ) binding pocket.
• Leupeptin is a competitive transition state inhibitor and its inhibition may be relieved by an excess of substrate.
• However, this result is controversial, as it is questionable if the leupeptin-induced material is true lipofuscin.
• For example, leupeptin could be used in a calpain extraction to keep calpain from being hydrolyzed by specific proteases.
• Amastatin, bestatin ( ubenimex ), leupeptin, and puromycin have been found to inhibit the enzymatic degradation of oxytocin, though they also inhibit the degradation of various other peptides, such as vasopressin, met-enkephalin, and dynorphin A.
• The accumulation of lipofuscin-like material may be the result of an imbalance between formation and disposal mechanisms : Such accumulation can be induced in rats by administering a protease inhibitor ( leupeptin ); after a period of three months, the levels of the lipofuscin-like material return to normal, indicating the action of a significant disposal mechanism.