Isolation and properties of two novel basic proteins from the outer layer of the vitelline membrane of hen's eggs
| Project/Area Number |
03808011
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
家政学
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| Research Institution | Kyoto Women's Junior College |
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Principal Investigator |
KIDO Shoko Kyoto Women's Junior College, Department of Living Science, Associate Professor, 生活科学科, 助教授 (40153150)
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| Project Period (FY) |
1991 – 1992
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| Project Status |
Completed (Fiscal Year 1992)
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| Budget Amount *help |
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1992: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1991: ¥1,000,000 (Direct Cost: ¥1,000,000)
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| Keywords | Vitelline Membrane / Basic Protein / Primary Structure / Secondary Structure / Disulfide Bonding / SーS結合 / 糖合成活性 / モノクロナ-ル抗体 |
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| Research Abstract |
Two basic proteins (named as VMOI and VMOII) were isolated from the outer layer of vitelline membrane and their protein structures and properties were investigated.
1.The complete amino acid sequence of VMOI has been deduced from the sequence analysis of fragments obtained by cleavage with several peptitases. VMOI is composed of 163 amino acid residues with a calculated molucular weight of 17,979. The peculiar CD spectra of VMOI at 23ﾟC was indicated that a spacial arrangement of aromatic side chains and a rich beta-structure are present in the native conformation and the structure unfold to unordered conformation at 70ﾟC. The Thermal stability of VMOI was measured by DSC analysis and the value of 67.5ﾟC for transition temprature was obtained and 52ﾟC in the presence of reductant. (2 in Biochemistry, 1993, in preparation)
2.The further basic protein, VMOII (pI 11.5), in the outer vitelline membrane was purified by ionexcharge chromatography. The amino acid composition of VMOII was characterized by the absence of Met and high contents of half-Cys (14%) and basic amino acids (15%) and all Cys were involved in disulfide bonding. The heat-resistance of VMOII was also confirmed by the thermal analysis of CD measurements and a property as cysteine peptitase inhibitor by the examination of proteolytic digestion. (Biochemical Journal, 1992)
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Report
(3 results)
Research Products
(8 results)
