Purification and cDNA Cloning of an Antifungal Protein from the Hemolymph of Holotrichia diomphalia Larvae

So young Lee, Hyun joo Moon, Bok luel Lee, Shoichiro Kurata, Shunji Natori

Research output: Contribution to journalArticlepeer-review

66 Citations (Scopus)

Abstract

An antifungal protein (AFP), holotricin 3, was purified from the hemolymph of the coleopteran insect Holotrichia diomphalia larvae. Analysis of its cDNA showed that holotricin 3 is a novel Gly- and His-rich protein consisting of 84 amino acid residues. This protein was similar to AFP, an antifungal protein of Sarcophaga peregrina that was reported previously, in terms of molecular size and high content of Gly and His residues. However, no appreciable sequence similarity was detected between the two proteins.

Original languageEnglish
Pages (from-to)1049-1052
Number of pages4
JournalBiological and Pharmaceutical Bulletin
Volume18
Issue number8
DOIs
Publication statusPublished - 1995

Keywords

  • Gly-
  • His-rich protein
  • antifungal protein
  • insect

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

Fingerprint Dive into the research topics of 'Purification and cDNA Cloning of an Antifungal Protein from the Hemolymph of Holotrichia diomphalia Larvae'. Together they form a unique fingerprint.

Cite this