Molecular properties and tissue distribution of 30K proteins as ommin-binding proteins from diapause eggs of the silkworm, Bombyx mori

We previously reported the purification of an ommin-binding protein (OMBP) from an acid-methanol extract of diapause eggs of the silkworm and that OMBP reacted with the anti-30K proteins antiserum. In order to clarify the relationship between OMBP and the 30K proteins, we attempted to determine the...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2007-02, Vol.146 (2), p.172-179
Main Authors: Sawada, Hiroshi, Yamahama, Yumi, Mase, Keisuke, Hirakawa, Haruka, Iino, Teruhiko
Format: Article
Language:English
Subjects:
30K proteins
Amino Acid Sequence
Animals
Bombyx - genetics
Bombyx - metabolism
Bombyx mori
Diapause eggs
Electrophoresis, Gel, Two-Dimensional
Female
Glycoproteins - chemistry
Glycoproteins - genetics
Glycoproteins - metabolism
Immunoblotting
Immunohistochemistry
Insect Proteins - chemistry
Insect Proteins - genetics
Insect Proteins - metabolism
Molecular Sequence Data
Molecular Weight
Ommin
Ommochrome-binding protein
Ovum - metabolism
Phenothiazines - metabolism
Protein Binding
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Analysis, Protein
Serosa
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Summary:We previously reported the purification of an ommin-binding protein (OMBP) from an acid-methanol extract of diapause eggs of the silkworm and that OMBP reacted with the anti-30K proteins antiserum. In order to clarify the relationship between OMBP and the 30K proteins, we attempted to determine the sequence of the N-terminal amino acid of OMBP, which was separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). We observed ten protein spots of various isoelectric points; the spots corresponded with 30 kDa. Based on the sequence of the N-terminal amino acid (20 residues), the spots belonged to two kinds of 30K proteins (6G1 and 19G1), which are known as the major plasma proteins in the larval hemolymph of the silkworm. The proteins are expected to attach to polysaccharide because they reacted with concanavalin A and elderberry bark lectin. Immunohistochemical observations clarified that the proteins were localized in yolk granules and serosa in the diapause egg. These results suggest that OMBP is composed of 30K proteins which were modified with polysaccharides. In addition, the expression of 30K proteins mRNA was observed at early embryonic stage in diapause eggs by RT-PCR analysis. The 30K proteins as OMBP may play an important role in the transport and accumulation of tryptophan metabolites and ommochrome during the formation of serosa.
ISSN:1096-4959
1879-1107
DOI:10.1016/j.cbpb.2006.10.101