• Animal cells and systems
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• v.1 no.1
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• pp.71-75
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• 1997

Male specific protein (MSP) was identified and purified from the hemolymph of Galleria melloneffa L. by electrophoresis and anion exchange chromatography. MSP has a native molecular weight of 55 kDa as determined by gel filtration chromatography and consists of a single unit with the apparent molecular weight of 27 kDa and has the pl of approximately 5.8. MSP is present in the hemolymph from day 8 pupae throughout the male adult. MSP was also found in pupal fat body, adult fat body, and adult testis.

• Journal of Aquaculture
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• v.11 no.2
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• pp.271-278
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• 1998

To clarify characteristics of yolk protein of abalone, yolk protein was purified from the ovarian egg extracts of mature female Haliotis discus hannai by a gel chromatography of sepharose CL-4B. From the results of immuno-electrophoresis and Ouchterlony's diffusion test to male and female sera and ovarian egg extracts using antibodies raised against mature female and male sera and male sera and ovarian egg extrascts, it was identified that the mature female serum had female specific serum protein and its antigenecity shared with ovarian egg extracts. A single type of yolk protein was purified from ovarian egg extracts, and it was composed of two subunits. Their molecular weights were estimated to be approximately 166 KDa and 113 KDa by SDSPAGE. The antiserum against yolk proteins cross-reacted with a mature female specific serum protein and extracts of hepatopancreas of vitellogeing females, but did not reacted with extracts of hepatopancreas of mature male.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.04a
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• pp.81-81
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• 2003

Male-specific protein (MSP) is a soluble protein which is accumulated 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. Three internal amino acid sequences of MSP were obtained by the in-gel digestion method using trypsin because of its blocked N-terminus. (omitted)

• The Korean Journal of Food & Health Convergence
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• v.4 no.4
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• pp.18-25
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• 2018

Proteins play a key role in many functions such as metabolic activity, differentiation, as cargos and cell fate regulators. It is necessary to know about the markers involved in male fertility in order to develop remedies for the treatment of male infertility. But, the role of the proteins is not limited to particular function in the biological systems. Some of the proteins act as ion channels such as catsper and proteins like Nanos acts as a translational repressor in germ cells and expressed in prenatal period whose role in male fertility is uncertain. Rbm5 is a pre mRNA splicing factor necessary for sperm differentiation whose loss of function results deficit in sperm production. DEFB114 is a beta defensin family protein necessary for sperm motility in LPS challenged mice where as TEX 101 is a plasma membrane specific germ cell protein whose function is not clearly known u to now. Gpr56 is another adhesion protein whose null mutation leads to arrest of production of pups in rats. Amyloid precursor protein role in Alzheimer's disease is already known but it plays an important role in male fertility also but its function is uncertain and has to be considered while targeting APP during the treatment of Alzheimer's disease. The study on amyloid precursor protein in male fertility is a novel thing but requires further study in correlation to alzheimer's disease.

• The Zoological Society Korea : Newsletter
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• v.12 no.2
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• pp.118.2-118
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• 1995

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.254.2-254
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• 1995

• Proceedings of the Zoological Society Korea Conference
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• 1994.10a
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• pp.181.2-181
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• 1994

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.5
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• pp.432-442
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• 1992

To identify the histological site of synthesis of yolk protein precursor, vitellogenin, by immunocytochemical method in the freshwater crab Eriocheir japonicus, we purified the yolk protein, vitellin, from crude egg extracts, and prepared the anti-rabbit serum against vitellin. Then, the site of vitellogenin synthesis was demonstrated by immunotytochemical method with PAP(peroxidase-antiperoxidase) reaction using the rabbit antiserum aganist vitellin. Female specific serum protein was identified in female serum by immunoelectrophoresis and Ouchterlony's immunodiffusion test for mature male and female sera. Based on the immunoelectrophoresis and Ouchterlony's diffusion test for mature male and female sera and crude egg extracts using antiserum against vitellogenic female serum absorbed with male serum, the female specific serum protein was identified as vitellogenin, detected in female serum only. The major yolk protein, vitellin, was purified from the crude egg extracts by DEAE-cellulose ion exchange chromatography, followed by sepharose CL-4B gel filteration chromatography. The molecular weight of vitellin was estimated to be about 245,000 dalton by sepharose CL-4B gel filteration chromatography. from the results of immunological analysis for vitellin, it was found that the vitellin antiserum contained the antibody against vitellogenin. In the results of immunocytochemical reaction by PAP method with the rabbit antiserum against vitellin, the vitellogenic oocytes and the hepatopancreas of mature female showed positive PAP reaction, but not in follicle cells and previtellogenic oocytes nf ovary, muscle of female and mature male hepatopancreas. Therefore, it showed that the hepatopancreas of mature female is the site of vitellogenic synthesis.

• Proceedings of the Korean Society of Applied Entomolohy Conference
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• 2002.05a
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• pp.175-175
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• 2002

• Proceedings of the Zoological Society Korea Conference
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• 1996.10a
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• pp.174.1-174
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• 1996

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