z-logo
Premium
A diapause associated protein of the pink bollworm Pectinophora gossypiella saunders
Author(s) -
Salama Mohamed S.,
Miller Thomas A.
Publication year - 1992
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940210102
Subject(s) - hemolymph , diapause , pink bollworm , biology , instar , larva , amino acid , biochemistry , botany
A diapause associated protein was electrophoretically isolated from the hemolymph of diapausing last instar larvae of the pink bollworm Pectinophora gossypiella . This protein (M r ∼490,000, glycolipoprotein) was given the name Pectinophora diapause protein (PDP). It is composed of one subunit (M r 103,000). The concentration of PDP increased dramatically in the hemolymph of diapausing larvae from 17.4% in prediapause (PD) phase to 29.2% in early diapause (ED) phase reaching a level of 38.6% in larval hemolymph of middiapause (MD) phase. The concentrations of total proteins in the hemolymph of active feeding (A), PD, ED, and MD larvae were 69.8, 106.6, 113.3, and 118 mg/ml, respectively, while those in the fat body of the same larvae were 7.1, 7.4, 8.8, and 4.5 mg/g, respectively. In Pectinophora a drop in the concentration of fat body proteins coincided with a corresponding increase in hemolymph proteins, which suggests an active release of protein from the fat body into the hemolymph during the development of diapause. A partial amino acid sequence of pectinophorin showed the first 15 amino acids starting from the amino terminus of the peptide chain: N‐ALA‐LYS‐THR‐ILEU‐VAL‐GLU‐ASN‐MET‐PRO‐PRO‐THR‐PRO‐LEU‐ASN‐ALA‐C. © 1992 Wiley‐Liss, Inc.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom