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

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 p...

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Bibliographic Details
Published in:Biological & pharmaceutical bulletin 1995/08/15, Vol.18(8), pp.1049-1052
Main Authors: LEE, SoYoung, MOON, HyunJoo, KURATA, Shoichiro, NATORI, Shunji, LEE, BokLuel
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antifungal Agents - isolation & purification
antifungal protein
Base Sequence
Biological and medical sciences
Cloning, Molecular
Coleoptera
Coleoptera - metabolism
DNA, Complementary
General pharmacology
Gly-, His-rich protein
Hemolymph - metabolism
insect
Insect Hormones - genetics
Insect Hormones - isolation & purification
Insect Proteins
Larva - metabolism
Medical sciences
Molecular Sequence Data
Pharmacognosy. Homeopathy. Health food
Pharmacology. Drug treatments
Scarabaeidae
Sequence Homology, Amino Acid
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Description
Summary: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.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.18.1049