PURIFICATION AND PROPERTIES OF A LIPID TRANSFER PARTICLE FROM BOMBYX-MORI - COMPARISON TO THE LIPID TRANSFER PARTICLE FROM MANDUCA-SEXTA

Authors
TSUCHIDA K SOULAGES JL MORIBAYASHI A SUZUKI K MAEKAWA H WELLS MA
Citation
K. Tsuchida et al., PURIFICATION AND PROPERTIES OF A LIPID TRANSFER PARTICLE FROM BOMBYX-MORI - COMPARISON TO THE LIPID TRANSFER PARTICLE FROM MANDUCA-SEXTA, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1337(1), 1997, pp. 57-65
Citations number
17
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1337
Issue
1
Year of publication
1997
Pages
57 - 65
Database
ISI
SICI code
0167-4838(1997)1337:1<57:PAPOAL>2.0.ZU;2-M
Abstract
A lipid transfer particle (LTP) was purified from the hemolymph of the silkworm Bombyx mori. Like other insect LTPs, the B. mori LTP is a ve ry high density lipoprotein containing 21% lipid and three apoproteins of mass approximate to 350 kDa, approximate to 85 kDa, and approximat e to 60 kDa. B. mori LTP catalyzes the exchange of lipids between diff erent density class lipoproteins found in adult hemolymph and between adult lipoproteins and vitellogenin. However, in no case was net lipid transfer observed. Manduca sexta LTP also catalyzed exchange of lipid s, but not net transfer of lipids, between different density class lip oproteins found in adult hemolymph.