波尔山羊杂交后代肉质特性的研究

随机选择相同放牧条件下的 6只波尔山羊与南江黄羊的杂交一代 (BN) ( 3♂、3♀ )以及同龄的南江黄羊 (NN) ( 3♂、3♀ )于 8月龄进行屠宰 ,提取肉样对肌肉品质进行分析。结果表明 ,BN保持了NN肉质细嫩多汁的优点 ,两者肌肉的失水率、系水力、贮存损失、熟肉率、肌肉剪切值和肌纤维直径等物理性状和肌肉的常规化学成分差异不显著 (P >0 .0 5)。通过风味品尝 ,不能辨别两者区别。BN肌肉蛋白质中的氨基酸种类齐全 ,含量丰富 ,赖氨酸、苯丙氨酸和蛋氨酸等人体必需氨基酸的含量还有所提高     

营养水平对肉鸡肌肉组织学的影响

试验设计了 9种能量或蛋白质水平不同的饲粮 ,研究了不同营养水平对肉鸡胸肌组织学的影响。结果表明 :饲粮能量或蛋白质水平增加 ,肉鸡胸肌纤维密度减小、直径增大 (P <0 0 1 )。所有处理中 ,高能中蛋白组试鸡胸肌纤维密度最小、直径最大 ,低能低蛋白组试鸡胸肌纤维密度最大 ,高能低蛋白组试鸡胸肌纤维直径最小。     

春小麦高蛋白品系F93-486主要性状的遗传研究

以高蛋白品系Ｆ９３－４８６为母本，武春１号和陇春８号为父本组配了２个组合，在每个组合中获得Ｐ１、Ｐ２、Ｆ１、Ｆ２、Ｂ１和Ｂ２６个群体，并以此为供试材料对Ｆ９３－４８６的蛋白质含量，角质率等性状的遗传规律进行了研究。     

肉用仔鸡主要营养、环境因素产量函数模型的研究

利用二次回归通用旋转组合设计对500只印第安河肉鸡生产的主要营养、环境因素进行了研究,建立了肉鸡生产函数模型,探讨了印第安河肉鸡日粮中粗蛋白质、代谢能水平及饲养密度等主要营养、环境因素及其相互效应和增重的关系,寻求了肉鸡增重最佳饲养管理措施组合方案和最优化的生产条件,为我国肉鸡生产技术的规范化提供了科学依据。肉鸡生产函数模型。y=2105.57+101.35X_1+42.93X_2-16.68X_3-16.3X_1X_2-99.47X_1~2-54.91X_2~2-51.16X_3~2。各因素对产量贡献大小顺序为粗蛋白质>代谢能>饲养密度。预测56日龄增重达1900克和净收入高于2.20元/只以上时,前期日粮需粗蛋白质21.55～22.37％,代谢能12.199～12.597MJ/kg,饲养密度32.9～34.4只/m~2;后期依次为19.55～19.76％,12.46～12.85MJ/kg,16.7～17.9只/m~2。蛋白质和代谢能存在交互作用。     

桃水溶性蛋白质等电聚焦电泳分析初报

对不同 pH 范围的两性载体电解质(Ampholine)进行等电聚焦(IEF)电泳,能获得不同的水溶性蛋白质谱型.结果表明:1.桃大多数器官酸性蛋白质含量丰富,宜选用pH3.5—7.0的 Ampholine 进行 IEF 电泳.2.桃不同器官水溶性蛋白质谱型差异显著.宜用花药、幼叶、叶柄、花瓣作为 IEF 电泳的主要分析器官;成熟叶、萼筒、种子作为辅助分析器官.3.萼筒和花瓣水溶性蛋白质谱型可鉴别黄肉桃、白肉桃两类品种,而花瓣谱型亦能区分桃大花、小花两种类型.     

饲粮蛋白质水平对早期断奶仔猪氮代谢的影响

选择30头28日龄断奶仔猪（平均体重4．5kg），研究饲粮粗蛋白质（CP）水平对早期断奶仔猪氮代谢的影响。结果显示：（1）饲粮CP水平分别与CP摄入量、CP表现消化率、可消化CP摄入量、未消化CP摄入量存在显著（P＜0．05）或极显著（P＜0．01）的正相关；（2）CP真消化率不受饲粮CP水平的影响，两者的相关关系不显著（P＞0．05）；（3）仔猪内源粪氮排泄量为0．22g／日，内源粪氮占干物质摄入量的比值为2．6g／kg；（4）饲粮CP水平分别与盲肠内容物中挥发性盐基氮（VBN）和氨氮（AN）含量的相关关系不显著（P＞0．05），但饲粮CP水平分别与结肠内容物中VBN和AN含量存在显著（P＜0．05）的正相关；（5）饲粮CP水平分别与血浆VBN和尿素氮含量存在显著（P＜0．05）和极显著（P＜0．01）的正相关，但血浆AN含量则不受饲粮CP水平的影响，两者的相关关系不显著（P＞0．05）。结果表明，随着饲粮CP水平升高，CP的真消化率不变，进入大肠的蛋白质量增加，结肠内蛋白质的腐败作用增强，血中含氮代谢产物增多。     

Interaction of bovine immunoglobulin gamma 2 (IgG2) with staphylococcal protein A: evidence for IgG2a and IgG2b sub-subclasses in the bovine

The reactivity of bovine IgG with protein A is confusing with respect to which of the bovine IgG class and subclasses are reactive. We have, therefore, re-examined the interaction of bovine immunoglobulins with protein A. The results presented in this paper indicated that at pH 8.0 protein A binds only immunoglobulin of the IgG2 subclass. The bound IgG2 can be readily recovered from an immobilized protein A column at pH 5.0. Furthermore, the antigenic IgG2 eluted demonstrated two charged species which could readily be separated by ion-exchange chromatography. These results indicate that IgG2 in the bovine exists in two sub-subclasses, IgG2a and IgG2b. The two sub-subclasses of IgG2 could be rapidly isolated with a good yield in two-steps namely protein A affinity chromatography followed by ion exchange chromatography.     

Preparation of recombinant PTD-HSP27 and verification of its ability to penetrate the cell membrane of human lens epithelial cells and rabbit cornea

AIM: To construct the prokaryotic expression system containing protein transduction domain (PTD) with heat shock protein 27 (HSP27) in order to prepare and purify the recombinant protein, and to verify whether the recombinant protein PTD-HSP27 has the ability to penetrate the human lens epithelial cell (HLEC) membrane and the rabbit cornea. METHODS: The plasmid pKYB-PTD-HSPB1-6His was constructed by the technique of overlap extension PCR. The plasmid was transformed and PTD-HSP27 was purified through nickel affinity chromatography column and identified by Western blotting. PTD-HSP27-6His was labeled with the fluorescein isothiocyanate (FITC). The penetrating ability of PTD-HSP27 into HLECs and rabbit cornea was tested. RESULTS: The recombinant PTD-HSP27 plasmid was successfully cloned and effectively expressed. The correctness of the recombinant protein PTD-HSP27 was demonstrated. Fluorescence microscopic examination showed that PTD-HSP27-FITC was internalized by HLECs. Fluorescent labeled PTD-HSP27 was then observed in the rabbit aqueous humor. CONCLUSION: The recombined gene PTD-HSPB1 was constructed by overlap extension PCR technique and the PTD-HSP27 fusion protein was prepared and purified by nickel affinity chromatography column. Using the technique of PTD-fusion protein, HSP27 was transduced into HLECs and passed through the cornea.     

Advance in receptor type protein tyrosine phosphatase Q

Receptor type protein tyrosine phosphatase Q (PTPRQ) is an unusual protein tyrosine phosphatase that has intrinsic dephosphorylating activity for various phosphatidylinositiol and phospho-tyrosine substrates, especially the phosphatidylinositol activity. Recent data show that PTPRQ has an important role in various biological processes and is associated with some diseases. In this article, the structure and function of PTPRQ and the relationship between PTPRQ and diseases were briefly summarized.     

Promoting effect of botulinum neurotoxin serotype A heavy chain on neuritogenesis in cultured Neuro-2a cells

AIM: To observe the neuritogenic actions of botulinum neurotoxin serotype A heavy chain (BoNT/A HC) on cultured Neuro-2a cells and to investigate the related signaling mechanisms for the effect of BoNT/A HC. METHODS: Neuro-2a cells were treated with different doses of BoNT/A HC (0.01, 0.1, 1 and 10 nmol/L), and then the cells were harvested at 24 h, 48 h and 72 h of BoNT/A HC exposure for detecting the neurite length and the percen-tage of the cells with neuronal processes by immunofluorescence staining. The most efficient dose of BoNT/A HC was chosen for exposure to Neuro-2a cells as the above. Whole cell protein was harvested at different time points for detecting the protein levels of phosphorylated ERK1/2 (p-ERK1/2) and phosphorylated Akt (p-Akt) by Western blot. RESULTS: Low doses of BoNT/A HC stimulated the neurite outgrowth, and increased the percentage of the cells with neurites compared with the negative controls (P<0.05), especially in the group with 1 nmol/L of BoNT/A HC treatment. Meanwhile, the phosphorylation of ERK1/2 and Akt was increased after treated with BoNT/A HC. There was an increasing tendency for the phosphorylation of ERK1/2 after the exposure of the cells to BoNT/A HC. The obvious increase in p-ERK1/2 was seen from 60 min to 5 h with 1 nmol/L of BoNT/A HC treatment (P< 0.05), and the increased protein level of p-Akt was mainly observed at 15 min and 60 min (P<0.05). CONCLUSION: BoNT/A HC stimulates the neuritogenesis. The neuritogenic mechanism of BoNT/A HC on Neuro-2a cells might be realized by activation of the phosphorylation of ERK1/2 and Akt.