A sapecin homologue of Holotrichia diomphalia: purification, sequencing and determination of disulfide pairs

Biol Pharm Bull. 1995 Mar;18(3):457-9. doi: 10.1248/bpb.18.457.

Abstract

We purified and characterized a sapecin homologue, named holotricin 1, from the hemolymph of immunized larvae of a coleopteran insect, Holotrichia diomphalia. We determined its complete amino acid sequence and three disulfide pairs. Holotricin 1 consisted of 43 amino acid residues and showed potent antibacterial activity against gram-positive bacteria, but antibacterial activity against gram-negative bacteria was not obvious.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Coleoptera / chemistry*
  • Disulfides / analysis*
  • Disulfides / isolation & purification
  • Disulfides / pharmacology
  • Hemolymph / chemistry
  • Insect Hormones / analysis*
  • Insect Hormones / chemistry*
  • Insect Hormones / isolation & purification
  • Insect Hormones / pharmacology
  • Insect Proteins*
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid

Substances

  • Disulfides
  • Insect Hormones
  • Insect Proteins
  • holotricin 1 protein, Holotrichia diomphalia
  • sapecin protein, Sarcophaga