抗生素单剂与联合治疗社区获得性肺炎的临床疗效观察

目的:观察β内酰胺类联合大环内酯类与β内酰胺类单剂治疗社区获得性肺炎的临床疗效。方法:收集我院呼吸内科住院的社区获得性肺炎患者262例,随机分为单剂治疗组和联合治疗组。两组患者均给予抗感染、对症支持治疗,其中单剂治疗组抗生素采用β内酰胺酶类单剂治疗,联合治疗组采用β内酰胺酶类和大环内酯类联合治疗。所有患者统计年龄、性别、基础疾病、病情严重程度,并记录治疗前与治疗后不同住院天数的血常规、C反应蛋白的变化,统计住院天数。结果:联合治疗患者一般基本情况(年龄、性别、基础疾病、病情严重程度)与单剂治疗组相比,P0.05,差异均无统计学意义。治疗前及治疗后首日C反应蛋白和白细胞计数二者相比,P0.05,差异均无统计学意义;联合治疗组与单剂治疗组相比,C反应蛋白在住院第2、4、6、9天,白细胞计数在住院第2、4、6天,均明显下降,住院天数缩短,P0.05,差异均有统计学意义。对于中、重度CAP(CRB65≥2),联合治疗组与单剂治疗组相比,治疗后C反应蛋白以及白细胞计数明显减少,P均0.05,差异有统计学意义;对于轻度CAP(CRB65=0~1),两组治疗后CRB和白细胞计数相比,P均0.05,差异无统计学意义。结论:β内酰胺类联合大环内酯类治疗治疗社区获得性肺炎临床疗效优于β内酰胺类单剂治疗。     

Proteomic analysis in the identification of allergenic molecules

Conventional and innovative strategies can be exploited to identify and characterize new allergenic proteins. With the aim of obtaining suggestions for future improvements, this article describes our attempt to understand and describe some of the advantages and pitfalls of the methodologies and procedures often used in this field. The analysis includes the protein extract preparation, starting from the allergenic source, the separation of the proteins contained in a mixture and the detection, identification and characterization of IgE-binding molecules. Classic and emerging proteomic technologies, including mass spectrometry-based methodologies, Edman degradation procedure, microarray-based techniques and bioinformatics search strategies, have been explored. A comparative analysis of biochemistry-based proteomics and molecular biology strategies has also been given.     

Enzyme antigens associated with pigeon breeder's disease. I. Isolation and characterization of basic hydrolases

A survey of the hydrolytic enzymes present in pigeon dropping extracts (PDE) has shown that this material contains a variety of proteolytic and nonproteolytic activities. These enzymes were separated into their basic and acidic components by chromatography on DEAE-cellulose. Staining of immunoprecipitates with specific chromogenic substrates demonstrated the presence of antibodies in symptomatic breeders to several of the basic enzymes in PDE. Five distinct hydrolytic activities were isolated from the basic group of enzymes. Trypsin, elastase, and two forms of collagenase were the specific proteolytic activities isolated. A phospholipase was also purified from these preparations. The purified elastase consisted of a single polypeptide chain (M _r =22,000). The purified trypsin had a molecular weight (M _r =25,000) and charge similar to those reported for elastase and, like elastase, the trypsin from PDE appeared to be composed of a single polypeptide chain. Two molecular weight forms of collagenase were found; both hydrolyzed bovine collagen. The high-molecular-weight collagenase (M _r =51,000) was shown to be a glycoprotein consisting of two polypeptides (M _r =24,000). It was readily separated from the low-molecular-weight collagenase (M _r =15,000) by gel filtration. The phospholipase (M _r =99,000) appeared to be a dimer. The relevance of these enzymes to the development of pigeon breeder's disease is discussed.     

Transgenic ryegrasses (Lolium spp.) with down-regulation of main pollen allergens

Ryegrass pollen (Lolium species) is a widespread source of air-borne allergens and is a major cause of hayfever and seasonal allergic asthma, which affect approximately 25% of the population in cool temperate climates. The main allergens of ryegrass pollen are the proteins Lol p 1 and Lol p 2. These proteins belong to two major classes of grass pollen allergens to which over 90% of pollen-allergic patients are sensitive. The functional role in planta of these pollen allergen proteins remains largely unknown. Here we describe the generation and analysis of transgenic plants with reduced levels of the main ryegrass pollen allergens, Lol p 1 and Lol p 2 in the most important worldwide cultivated ryegrass species, L. perenne and L. multiflorum. These transgenic plants will allow the study of the functional role in planta of these pollen proteins and the determination of potential for development of hypo-allergenic ryegrass cultivars.