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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.
Q. Diagnosis of diabetes mellitus? Timely and proper diagnosis plays a key role not only in identifying new cases but also in managing old cases with or without diabetic compli
Briefly explain the difference between stabilizing selection, directional selection, and disruptive selection.
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Most of the coronary blood flow to the left ventricular myocardium occurs during diastole. Thus the contracting heart obstructs its own blood supply. The systolic compressive force
Feeding mechanism in holozoic animal
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