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Elastase
The inactive proelastase is activated by trypsin to the active form elastase. Elastase attacks peptide bonds next to the small amino acid residues such 3s glycine, alanine and serine and has a broader specificity than the other two enzymes.
All the three enzymes viz. trypsin, chymotrypsin and elastase are endopeptidases (a subclass of peptide hydrolases that hydrolyse the more centrally situated peptide bonds). You have already seen that pepsin is also an endopeptidase.
What is Active site Active site : The site on the surface of an enzyme to which substrate or substrates bind.
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sturucture explain
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Golgi complex is the organelles in animal cells having a sequence of þattened sacs which sort, chemically modify, and package proteins produced on the rough endoplasmic reticulum.
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