Evidences for a stage-specific juvenile hormone binding protein in the hemolymph of the silkworm,Bombyx mori L.: Identification and characterization by photoaffinity labeling and immunological analyses

Park, Chul Ho; Kim, Hak R.

doi:10.1002/(sici)1520-6327(1996)33:2<83::aid-arch1>3.0.co;2-y

Cited by 2 publications

(4 citation statements)

References 30 publications

(19 reference statements)

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“…The constant levels of 32 kDa in haemolymph until wandering (Fig. 4b) are very similar to the constant levels of the 33 kDa protein in haemolymph (Park & Kim, 1996). The 35 kDa protein (Park & Kim, 1996) is present at lower levels than the 33 kDa protein and its physiological role remains to be determined.…”

Section: Discussionsupporting

confidence: 65%

“…hJHBP from B. mori in our study and that of Kurata et al . (1994) had a M r of 32 kDa (Figs 4c, 5), possibly being the same protein as the 33 kDa of Park & Kim (1996). The constant levels of 32 kDa in haemolymph until wandering (Fig.…”

Section: Discussionmentioning

confidence: 86%

“…In a study by Park & Kim (1996), two molecular forms of hJHBP were found in B. mori haemolymph by photo‐affinity labelling. One form, with a M r of 33 kDa, was present at constant levels in 3rd to 5th instar haemolymph, while the other form of 35 kDa was detected only in haemolymph until the early 5th instar (Park & Kim, 1996). The two forms were immunologically similar, although whether they represent the same original polypeptide and are differently processed remains unknown.…”

Section: Discussionmentioning

confidence: 99%

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The juvenile hormone binding protein of silkworm haemolymph: gene and functional analysis

Vermunt

Kamimura

Hirai

et al. 2001

Insect Molecular Biology

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A cDNA fragment of haemolymph juvenile hormone binding protein (hJHBP) from larvae of Bombyx mori was amplified by RT-PCR using degenerate primers based on the N-terminal amino acid sequence of purified hJHBP and a conserved region near the C-terminus of other lepidopteran hJHBPs. 5'- and 3'-ends were amplified by RACE to yield cDNAs, hJHBP1 and hJHBP2, encoding 225 amino acids with three substitutions. hJHBP-mRNA levels in the fat body were constant in the 4th instar, but decreased in the 5th. JHBP protein was constant until wandering, then declined. Recombinant hJHBP1 expressed in E. coli migrated on SDS-PAGE with a Mr of 32 kDa and showed a Kd of 4.5 x 10-7 M with JH III, both similar to those of native hJHBP.

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Section: Discussionsupporting

confidence: 65%

Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

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The juvenile hormone binding protein of silkworm haemolymph: gene and functional analysis

Vermunt

Kamimura

Hirai

et al. 2001

Insect Molecular Biology

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“…6). Each protein of MSP and JHBPs had a signal peptide region consisting of 18 amino acids, except G. mellonella JHBP that consisted of 20 amino acids, and was synthesized in the fat body, and then secreted into the hemolymph (Ozyhar and Kochman, Archives of Insect Biochemistry and Physiology 1987; Lerro and Prestwich, 1990;Wojtasek and Prestwich, 1995;Park and Kim, 1996;Vermunt et al, 2001;Parkitna et al, 2002). Four conserved cysteins found in JHBPs were also found in MSP.…”

Section: Cdna Sequence Of Mspmentioning

confidence: 99%

Cloning and expression of male‐specific protein (MSP) from the hemolymph of greater wax moth, Galleria mellonella L.

Han

Lee

Yun

et al. 2003

Arch Insect Biochem Physiol

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Male-specific protein (MSP) is a soluble protein that accumulates in high amounts in the hemolymph and other organs of adult male wax moth. The MSP was purified from adult male wax moth by gel filtration and reversed phase column chromatography, and its amino acid sequence was determined. Because of blocked N-terminus, several internal amino acid sequences of MSP were obtained by the in-gel digestion method using trypsin. RT-PCR was conducted using degenerate primers designed from the internal amino acid sequences. 5'-RACE PCR was used to obtain the complete coding region and 5'-UTR sequence. The full length MSP cDNA sequence encodes a 239 amino acid polypeptide with an 18 amino acid signal peptide. The putative mature MSP has a molecular mass of 24,317 Da and an isoelectric point (pI) of 6.00, but shows a molecular mass of 27 kDa on SDS-PAGE. Sequence alignment showed a significant similarity between MSP and juvenile hormone binding proteins (JHBPs) of several lepidopteran species, including G. mellonella.

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Evidences for a stage-specific juvenile hormone binding protein in the hemolymph of the silkworm,Bombyx mori L.: Identification and characterization by photoaffinity labeling and immunological analyses

Cited by 2 publications

References 30 publications

The juvenile hormone binding protein of silkworm haemolymph: gene and functional analysis

The juvenile hormone binding protein of silkworm haemolymph: gene and functional analysis

Cloning and expression of male‐specific protein (MSP) from the hemolymph of greater wax moth, Galleria mellonella L.

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