Roles of protein kinase C in oocyte meiotic maturation and fertilization

Protein kinase C (PKC) is a superfamily of Ser/Thr protein kinases that is distributed widely in eukaryotes. It plays key regulatory roles at multiple steps of oocyte meiotic maturation and fertilization. During the process of meiotic maturation, the activation of PKC in cumulus cells stimulates meiotic maturation, whereas the activation of PKC in oocytes results in the inhibition of germinal vesicle breakdown. PKC activity increases following the meiotic maturation, and decreases at the transition of metaphase/anaphase in meiosis I, so as to facilitate the release of the first polar body and the entry of meiosis II. In fertilization of mammalian oocytes, PKC may act as one of the downstream targets of Ca2+ to stimulate the cortical granule exocytosis, release the oocytes from MII arrest and to induce pronucleus formation. PKC is also involved in the regulation of maturation promoting factor (MPF) and mitogen-activated protein kinase (MAPK). Several PKC isoforms have been identified in mammalian oocytes, and there is evidence showing that classical PKCs may be the principal mediator of oocyte cortical reaction.     

Dependence of mutual information of big protein sequence

The mutual information function is used to describe the auto-correlation of amino acids in protein. We find two interesting phenomenon: (1) for any given big protein, the mutual information function l(k) is almost a const, where k is the length of gap. (2) for any two sequence similar proteins, the mutual information are nearly the same. As a consequent, we may use mutual information of protein as a character for sequences comparison. Foundation item: Supported by the National Natural Science Foundation of China (30170214) Biography: Shi Feng ( 1966-), male, Ph. D, Associate professor, research direction: bioinformatics.     

N-terminal of L protein of vesicular stomatitis virus contains a new signal sequence

The L protein (241kD) of vesicular stomatitis virus (VSV) is the most important snbnnit of the replication complex. The existence of specific localization signal in the L protein was investigated by making recombinant constructs expressing truncated mutants of the L protein fused to green fluorescent protein (GFP) in transient transfection assays. The chimeric genes encoding varied N-terminal of L and GFP gene were put under the control of T7 promoter or CMV promoter. The fusion proteins were transiently expressed in BHK-21, COS-7, CHO or Hep G2 cells. When more than 120 residues were deleted or only 96 residues were kept on the N-terminal, the fusion proteins were shown to be distributed throughout the cells, cytoplasm and nucleus under the confocal microscope. However, other chimeric proteins with 120 or more amino acids were dotted and distributed in the perinuclear regions. And the fusion protein with 96—120 aa has the similar distribution. A thirteen-residue peptide QGYSFLHEVDKEA (108—120) was identified as localization signal, whose function would be absolutely distributed with the deficiency of D or V. Our results show that there is an independent localizing signal in N-terminal domain of L protein of VSV and this functional signal is conserved in different cell lines.     

Analysis of cDNA sequence, protein structure and expression of parotid secretory protein in pig

Parotid secretory protein (PSP) secreted abundantly in saliva, whose function is related with the anti-bacterial effect. The PSP cDNA has been isolated from pig parotid glands by 3′ and 5′ rapid amplification of cDNA end (RACE), based on the conserved signal peptide region among the known mammalian PSP. The result of homologous comparison shows that pig PSP and human PSP shares the high identity at the level of the primary, secondary and tertiary protein structure. A search for functionally significant protein motifs revealed a unique amino acid sequence pattern consisting of the residues Leu-X(6)-Leu-X(6)-Leu-X(7)-Leu-X(6)-Leu-X(6)-Leu near the amino-terminal portion of the protein, which is important to its function. RT-PCR, Dot blot and Northern blot analysis demonstrated that PSP was strongly expressed in parotid glands, but not in other tissues.     

Inhibitory effect of the adenovirus type 5 E1A protein expressed in the yeast system of the human tumor cell growth

Adenovirus 5 type E1A as a tumor suppressor gene can inhibit tumor growth and enhance the censitivity of chemotherapy and radiotherapy.E1A have the ability to integrate into the host genome,resulting in long-time expres-sion that induces Rb gene inactivation and animal cells im-mortalization.This prompted us to select the E1A protein for treatment of cancer in order to overcome the limitations of E1A gene therapy.Thus,we firstly comstructed E1A eu-caryotic expression vector (pPIC9/E1A),transformated the pichia pastoris yeast cells(GS115) and screened the high-expressing recombinant strains.The positive yeast strains were cultured in the shake flask,and induced for 3d.The crude E1A protein was purified using two steps of col-umu chromatography on HiTrap Q and HiTrap SP.The pu-rified E1A protein was identified by SDS-PAGE and Western blot.E1A protein was mostly located at cellular unclear when Cheriot delivered E1A protein into cells.The analysis in vitro indicated that the E1A protein arrested LN686 cell cycle at G2/M phase,and significantly inhibited the growth of LN686 tumor cells.The current studies firstly provided an experimental basis to further develop E1A protein for tumor treatment.     

大豆蛋白纤维纱线的漂白处理

探讨和比较了氧化法漂白和氧化·还原法漂白两种漂白工艺.在氧化法漂白工艺中,分析了温度、H2O2浓度和时间三种重要参数对漂白效果的影响规律,得出了白度能满足染色要求的两种漂白工艺.     

新疆北鲵肌肉蛋白质、氨基酸、无机元素及食物组成分析

本报道了新疆北鲵肌肉蛋白质含量为19．08％，氨基酸17种，无机元素有Ca等6种，成幼体食物组成中以石蚕及腺状介虫为主．     

利用猪粪集约化生产蝇蛆的生态工程研究

利用蝇蛆对猪粪的能量、物质进行消化吸收，在集约化生产条件下获得生物肥及蝇蛆蛋白两个产品．结果表明，蝇蛆生物肥为咖啡色、无奥和疏松状，其肥效指标明显优于自然熟化的猪粪，氮含量显著优于干猪粪；蝇蛆干品的氨基酸总量、粗脂肪含量、粗纤维和灰分含量等指标均优于鱼粉．蝇蛆处理猪粪具有提高生产利润、净化生产环境等一系列经济效益、社会效益和生态效益，具有农业生态工程的特点．     

酶法水解棉籽蛋白的制备与应用

以脱酚后的棉籽粉为原料 ,研究了酶解法制备可溶性棉籽水解蛋白的生产工艺。对其影响因素和产品的实际应用作了探讨。结果表明 ,利用中性蛋白酶AS1.398水解棉籽粉 ,产品得率可达 28.8%,蛋白质量分数为63.28%。棉籽水解蛋白可作为菌体发酵氮源。