• Journal of Sericultural and Entomological Science
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• v.29 no.2
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• pp.38-43
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• 1987

The just molted larvae of the fifth instar were fed on with cadmium trated mulberry leaf and on the third day of the fifth instar the daily change of the total protein, activities of GOT and GPT in larvae haemoymph were sexually analyzed. The result obtained are summarized as follows : 1. The total haemolymph was decreased by cadmium treatment. A decreasing ratio of the total haemolymph protein was higher at the later development stage of the male fifth instar than the female fifth instar. 2. There seemed a slight difference in albumin content of the female blood along with the fifth larvae development between control and cadmium treatment where 7% decrease of blood albumin took place with cadmium treatment comparing to that of cotrol. Contrarily a decrease of blood globulin was made on both sexes. 3. The activities of GOT and GPT were inhibited by cadmium treatment.

• Journal of Sericultural and Entomological Science
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• v.28 no.1
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• pp.37-42
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• 1986

The experiment was carried out to investigate the effects of juvenile hormone analogue on changes of protein and amino acids in haemolymph of silkworm larva. Juvenile hormone analogue was topically administered to larvae at dose of 1$\mu\textrm{g}$ 10$\mu\textrm{g}$ per gm of body weight at 60hr. of the 5th instar. The results obtained were as follows ; 1. Larval duration of the fifth instar was extended about 1 day by JHA-1 and 4 days by JHA-10 as compared with the control. 2. Cocoon weight and cocoon layer weight by topical application of JHA were heavier than those of the control, but cocoon layer ratio was decreased in JHA-10 to the exclusion of JHA-1. 3. The concentration of haemolymph protein during the fifth instar was increased remarkably by the JHA application. 4. The total content of amino acids in haemolymph proteins of JHA-10 approximately doubled that of the control, with the conspicuous increase of glycine and arginine level.

• Animal cells and systems
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• v.3 no.1
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• pp.47-52
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• 1999

Change of proteins was confirmed during low temperature acclimation of overwintering larva, and some biochemical characteristics of the induced antifreeze protein-1 (AFP-1) were investigated in Protaetia brevitarsis. As the freezing point depression by the action of induced AFPs, a considerable thermal hysteresis was observed in the haemolymph and in partially purified proteins. AFP-1 was purified from the cold acclimation larvae by ammonium sulfate precipitation ion exchange chromatography, gel permeation chromatography, and electroelution. The purified AFP-1 was determined to be a glycoprotein (approximately 320 kDa, pl 5.8) composed of a single type of subunit (80 kDa). The high contents of hydrophilic amino acids (Asp, Glu, Lys, Asn, Gln, Arg, Ser, Thr) were also confirmed, showing similarity with antifreeze proteins from other insects.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2002.05a
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• pp.168-168
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• 2002

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2002.04a
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• pp.48-48
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• 2002

• Journal of Sericultural and Entomological Science
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• v.40 no.1
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• pp.43-51
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• 1998

Studies were carried out to investigate phenotypic expression, mortality and biochemical analysis of haemolymph proteins of nm-d, nm-f, nm-k and nmn bib-molting mutants of the silkworm, Bombyx mori. The non-molting mutants characters were expressed in the homozygote of each mutant genes. All strains of non-molting mutants were similar with each other in physiological characteristics, but the expression varied with each strains. The larvae of nm-d, nm-i and nmn died between day 5 and day 9 after hatching without the first molt. The nm-f and nm-k mutants died between day 5 and day 16 with a slight increase of body weight and, more than 90% of the mutants larvae died before the first molt and a few of them survived to the 2nd and the 3rd instar and died. The haemolymph protein components of nm-d, nm-i, and nmn were rapidly reduced, and on the other hand those of nm-f and nm-k consistently until they died. And there were no distinguishable difference in haemolymph components of non-molting mutants, as compared to those normals.

• Journal of Sericultural and Entomological Science
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• v.34 no.1
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• pp.30-34
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• 1992

Isolation, purification and molecular properties of adult specific protein (ASP) were investigated in the silkworm, Bombyx mori. ASP was purified from adult haemolymph by gel filtration on Sephadex G-100 and ion exchange chromatography on CM52. The preparation was shown to be homogeneous by native-PAGE and immunoelectrophoresis. The purified protein was consisted of two different subunits with molecular weights of 19.5kDa and 17.5kDa, and contained no sugars and no lipids.

• The Korean Journal of Zoology
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• v.17 no.2
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• pp.81-92
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• 1974

The blood proteins of pine moth, Dendrolimus spectabilis Butler of different developmental stages were investigated by disc electrophoresis in acrylamide gels. Blood protein concentration was also determined during the metamorphosis. Protein concentration increased gradually with the growth of larva, reaching a maximum in themature larva, and the increase of protein bands also was accompanied. As the larva transforms into the prepupa the number of protein bands as well as the protein concentration dropped. A total of 22 bands were identified throughout the stages. Histochemical staining of the acrylamide gels by the PAS method, Toluidine blut O, and Sudan black demonstrated that the carbohydrate, mucopolysaccharide, and lipid were associated with certain blood proteins.

• International Journal of Industrial Entomology and Biomaterials
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• v.8 no.2
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• pp.189-194
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• 2004

Amylase isozyme based three multivoltine viz., N+p, Np, N+ $p^{cho}$ and two bivoltine-D6+p, D6p syngenic lines (Syn. L) were developed from germplasm (GP) stocks Nistari (N) and D6 respectively. haemolymph isozyme pattern at pH 7.0 and 8.5 depicted a total 11 number (Am $y_{1 to 6}$ at pH 7.0 and Am $y^{l to 5}$ at pH 8.5) of native proteins (NP) of various sizes are amylase isozyme expressers. Among eleven NPs, two NPs of 770 kDa (Am $y^{6}$ at pH 7.0) and 376 kDa (Am $y^3$ at pH 8.5) are $\alpha$-amylase expressers and remaining NPs of 370, 364, 350, 329 and 274 kDa at pH 7.0 and 206, 292, 416, 725 kDa at pH 8.5 are $\beta$-amylase expressers. Accordingly, digestive juice amylase isozyme pattern at aforesaid pH also depicted a total number of 10 NPs (Am $y^{1 to 5}$) at each pH 7.0 and 8.5 are amylase expressers of which NP of 387 kDa (Am $y^4$ at pH 7.0) and 780 kDa (Am $y^{5}$ at pH 8.5) are a-amylase expresser. Remaining NPs of 338,297 ＆ 216 kDa at pH 7.0 and 370, 341, 329 ＆302 kDa at pH 8.5 are $\beta$-amylase expresser. Recurrent backcross lines (RBL) viz., N+pRBL and NpRBL were developed through introgression of high shell weight character (a multigenic trait) to be used further for congenic line (Con. L) development and to understand any association with introgressed character. Isozyme pattern in haemolymph of RBLs depicted only one $\alpha$-amylase of 770 kDa at pH 7.0 and 376 kDa at pH 8.0 with three and four respective $\beta$-amylase bands but in bivoltine lines numbers of $\beta$-amylase bands vary between 1 to 2 at aforesaid pH. Variability was also observed in digestive juice of multivolitine and its RBLs but bivoltine lines express null activity at both pH except appearance of one very week $\alpha$-amylase band D6+p at pH 8.5. Overall study suggests that not a single NP at both pH is common for expression of any band of amylase isozyme i.e., a totally different set of proteins are the amylase isozyme expresser at specific pH and no molecular factor of amylase is associated in developed RBLs which showed improvement on survival, single cocoon shell weight (SCSW) and single filament length over receptor parents.s.s.s.

• Journal of Life Science
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• v.18 no.3
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• pp.409-413
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• 2008

The occurences of proteins relating to Antheraea pernyi arylphorin in haemolymph, fat body, integument, midgut and silkgland of the wild silkmoths, Antheraea yamamai, Antheraea pernyi, Samia cynthia pryeri and Actias gnoma in the 5th larval instar were investigated by immunoblot analysis using mouse polyclonal antibody against A. pernyi arylphorin as probe. In A. yamamai, A. pernyi, S. cynthia pryeri and A. gnoma, the major immunoreactive antigenic proteins with a molecular weight of 80 KDa against the antisera of the A. pernyi arylphorin were clearly observed in the haemolymph, but in the integument, fat body, midgut and silkgland of the corresponding wild silkmoths the presence of the immunoreactive proteins were very variable. These results suggest that the A. pernyi arylphorin has almost same immunological identity with those of the wild silkmoths, A. yamamai, S. cynthia pryeri and A. gnoma though the distribution of the corresponding antigenic arylphorins is different according to the tissues of the wild silkmoths.