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Hypodermin B, a trypsin-related enzyme from the insect Hypoderma lineatum. Comparison with hypodermin A and Hypoderma
European Journal of Biochemistry
|August 1, 1983
Summary
Hypodermin B, a serine proteinase from Hypoderma lineatum larvae, exhibits trypsin-like activity and structural similarity to other serine proteinases. Its inhibition and specificity profile distinguishes it from Hypoderma collagenase.
Area of Science:
- Biochemistry
- Enzymology
- Parasitology
Background:
- Hypoderma lineatum larvae possess various enzymes, including serine proteinases.
- Previous isolation of hypodermin A and Hypoderma collagenase from these larvae.
Purpose of the Study:
- To purify and characterize hypodermin B, a serine proteinase from Hypoderma lineatum.
- To investigate its enzymatic activity, inhibition profile, and structural homology.
Main Methods:
- Purification of hypodermin B to homogeneity.
- Enzymatic assays using synthetic substrates.
- Inhibition studies with specific reagents and inhibitors.
- Amino acid composition and N-terminal sequencing.
Main Results:
- Hypodermin B is a serine proteinase (23000 MW) inhibited by DFP and specific lysine reagents.
- It hydrolyzes trypsin substrates but lacks chymotryptic activity.
- Exhibits broader specificity than bovine trypsin on insulin B chain.
- Shows structural homology with trypsin family and hypodermin A, differing from Hypoderma collagenase.
Conclusions:
- Hypodermin B is a trypsin-like serine proteinase.
- It shares similarities with hypodermin A but is distinct from Hypoderma collagenase.
- These findings contribute to understanding parasitic enzyme function and evolution.