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Patchwork-structure serpins from silkworm (Bombyx mori) larval hemolymph.

T Sasaki1

  • 1Department of Food Science and Technology, School of Agriculture, Nagoya University, Aichi, Japan.

European Journal of Biochemistry
|December 5, 1991
PubMed
Summary
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A novel silkworm antichymotrypsin II (sw-AchyII) was identified with antichymotryptic activity. This serine proteinase inhibitor features a unique reactive site, Phe340-Met341, and shows distinct sequence similarity to silkworm antitrypsin (sw-AT).

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Insect Physiology

Background:

  • Serpins (serine proteinase inhibitors) are crucial regulators of proteolytic activity.
  • Understanding insect serpins provides insights into evolutionary conservation and functional diversity of these proteins.

Purpose of the Study:

  • To isolate and characterize a novel antichymotryptic serpin from silkworm (Bombyx mori) larval hemolymph.
  • To determine the amino acid sequence and identify the reactive site of the newly discovered serpin, named silkworm antichymotrypsin II (sw-AchyII).

Main Methods:

  • Isolation and purification of sw-AchyII from silkworm hemolymph.
  • Amino acid sequencing of sw-AchyII using Edman degradation and mass spectrometry.
  • Analysis of complex formation and dissociation with alpha-chymotrypsin under varying pH conditions.

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Main Results:

  • A new serpin, sw-AchyII, composed of 375 amino acids without cysteine or glycosylation, was identified.
  • sw-AchyII formed an SDS-undissociable complex with alpha-chymotrypsin, cleaving at the Phe340-Met341 reactive site.
  • Sequence analysis revealed complete identity with silkworm antitrypsin (sw-AT) up to residue 336, but only 46% similarity thereafter, with reactive sites in variable regions.

Conclusions:

  • sw-AchyII is a distinct antichymotryptic serpin in silkworms with a uniquely identified reactive site.
  • The structural and sequence variations between sw-AchyII and sw-AT highlight functional specialization within silkworm serpins.