Lipophorin of the larval honeybee, Apis mellifera L.

Most insects have a major lipoprotein species in the blood (hemolymph) that serves to transport fat from the midgut to the storage depots in fat body cells and from the fat body to peripheral tissues. The generic name lipophorin is used for this lipoprotein. In larvae of the honeybee, Apis mellifera...

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Main Authors: S L Robbs, R O Ryan, J O Schmidt, P S Keim, J H Law
Format: Article
Language:English
Published: Elsevier 1985-02-01
Series:Journal of Lipid Research
Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520343947
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spelling doaj-5990b1617f0f4499873b2bacf561ef6d2021-04-25T04:15:42ZengElsevierJournal of Lipid Research0022-22751985-02-01262241247Lipophorin of the larval honeybee, Apis mellifera L.S L RobbsR O RyanJ O SchmidtP S KeimJ H LawMost insects have a major lipoprotein species in the blood (hemolymph) that serves to transport fat from the midgut to the storage depots in fat body cells and from the fat body to peripheral tissues. The generic name lipophorin is used for this lipoprotein. In larvae of the honeybee, Apis mellifera, a lipophorin has been found with properties that correlate well with those of the only other lipophorin reported for an immature insect, that of the tobacco hornworm, Manduca sexta. The honeybee lipophorin (Mr = 530,000) has a density of 1.13 g/ml, contains approximately 41% lipid and 59% protein, and contains two apoproteins, apoLp-I, Mr = 250,000 and apoLp-II, Mr = 80,000, both of which are glycosylated. The lipids consist predominantly of polar lipids, of which phospholipids and diacylglycerols represent 60% of the total. When the intact lipophorin is treated with trypsin, apoLp-I is rapidly proteolyzed, while apoLp-II is resistant, indicating a difference in exposure of the two apoproteins to the aqueous environment. Honeybee apoLp-II cross-reacts with antibodies to M. sexta apoLp-II, but not to anti-M. sexta apoLp-I. No cross-reactivity of honeybee apoLp-I to anti-M. sexta apoLp-I was observed.http://www.sciencedirect.com/science/article/pii/S0022227520343947
collection DOAJ
language English
format Article
sources DOAJ
author S L Robbs
R O Ryan
J O Schmidt
P S Keim
J H Law
spellingShingle S L Robbs
R O Ryan
J O Schmidt
P S Keim
J H Law
Lipophorin of the larval honeybee, Apis mellifera L.
Journal of Lipid Research
author_facet S L Robbs
R O Ryan
J O Schmidt
P S Keim
J H Law
author_sort S L Robbs
title Lipophorin of the larval honeybee, Apis mellifera L.
title_short Lipophorin of the larval honeybee, Apis mellifera L.
title_full Lipophorin of the larval honeybee, Apis mellifera L.
title_fullStr Lipophorin of the larval honeybee, Apis mellifera L.
title_full_unstemmed Lipophorin of the larval honeybee, Apis mellifera L.
title_sort lipophorin of the larval honeybee, apis mellifera l.
publisher Elsevier
series Journal of Lipid Research
issn 0022-2275
publishDate 1985-02-01
description Most insects have a major lipoprotein species in the blood (hemolymph) that serves to transport fat from the midgut to the storage depots in fat body cells and from the fat body to peripheral tissues. The generic name lipophorin is used for this lipoprotein. In larvae of the honeybee, Apis mellifera, a lipophorin has been found with properties that correlate well with those of the only other lipophorin reported for an immature insect, that of the tobacco hornworm, Manduca sexta. The honeybee lipophorin (Mr = 530,000) has a density of 1.13 g/ml, contains approximately 41% lipid and 59% protein, and contains two apoproteins, apoLp-I, Mr = 250,000 and apoLp-II, Mr = 80,000, both of which are glycosylated. The lipids consist predominantly of polar lipids, of which phospholipids and diacylglycerols represent 60% of the total. When the intact lipophorin is treated with trypsin, apoLp-I is rapidly proteolyzed, while apoLp-II is resistant, indicating a difference in exposure of the two apoproteins to the aqueous environment. Honeybee apoLp-II cross-reacts with antibodies to M. sexta apoLp-II, but not to anti-M. sexta apoLp-I. No cross-reactivity of honeybee apoLp-I to anti-M. sexta apoLp-I was observed.
url http://www.sciencedirect.com/science/article/pii/S0022227520343947
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AT roryan lipophorinofthelarvalhoneybeeapismelliferal
AT joschmidt lipophorinofthelarvalhoneybeeapismelliferal
AT pskeim lipophorinofthelarvalhoneybeeapismelliferal
AT jhlaw lipophorinofthelarvalhoneybeeapismelliferal
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