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METABOLISM OF ORAL BACTERIA

METABOLISM OF ORAL BACTERIA
口腔细菌的代谢
批准号:
3896733
负责人:
ROBERT J GENCO
金额:
$0.0万
依托单位国家:
美国
项目类别:
财政年份:
--
资助国家:
美国
项目状态:
未结题
起止时间:
至

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中文摘要
翻译
在两个主要领域开展了研究工作; 1. 表征厌氧生物作用对 革兰氏阴性兼性细菌的超微结构和表面蛋白 厌氧菌 研究结果表明,厌氧可能发挥作用, 在调节细菌表面成分中的重要作用。 这些研究的结果最近已经发表 (Infection and Immunity,1987,55:2320-2323)。 2. a. 主成分形成的表征 口腔革兰氏阳性菌唾液膜 和放线菌属)。 初步实验涉及 将各种口腔细菌菌株的纯培养物在 新鲜采集的人腮腺或下颌下-舌下 唾液,然后提取吸附的唾液 含2%SDS的组分。 唾液成分结合到 SDS-PAGE鉴定菌体表面, 免疫印迹。 唾液中的主要成分从 血链球菌为低分子粘蛋白 (MG2)和α-淀粉酶,而MG 2是主成分 从其它链球菌和A.粘性。 MG2, 从A.粘滞物随 电泳迁移率与去唾液酸-MG 2相似。 这些 通过检查以下因素之间的相互作用来验证观察结果: 125 I-HSMSL或125 I-HPS与几种试验菌株。 当 ~(125)I-唾液膜;采用SDS-聚丙烯酰胺凝胶电泳法分析血细胞。 PAGE/放射自显影,放射自显影图主要由 约55-60 kDa的组分,以及低的 分子量谱带 唾液膜 其他细菌含有多种其他成分, 分子量 这些数据表明, 在主要唾液分泌物和 测试的细菌菌株的表面。 一份手稿 正在编写这些调查结果的摘要。 B. 腮腺淀粉酶结合特性的研究 (同工酶B1)到S.血和其他口腔细菌。 纯化 淀粉酶(同工酶B1)从腮腺唾液中制备, 过滤色谱法,然后进行FPLC阴离子交换 层析 通过电泳评估纯度, 氨基酸分析 确定特异性的实验 ~(125)I标记淀粉酶B_1与S.血液和其他口服 细菌正在进行中。
英文摘要
Research efforts have developed in two major areas; 1. Characterization of the effect of anaerobiosis on the ultrastructure and surface proteins of gram-negative facultative anaerobes. Findings suggest that anaerobiosis may play an important role in the regulation of bacterial surface components. The results of these studies have been recently published (Infection and Immunity, 1987,55:2320-2323). 2. a. Characterization of the principal components forming the salivary pellicle on gram-positive oral bacteria (Streptococci and Actinomyces). Preliminary experiments involved the incubation of pure cultures of various oral bacterial strains in freshly collected human parotid or submandibular-sublingual saliva, followed by the extraction of adsorbed salivary components with 2%SDS. Salivary components bound to the bacterial surface were identified by SDS-PAGE and immunobloting. The principal salivary components eluted from Streptococcus sanguis were the low molecular weight mucin (MG2) and alpha-amylase, while MG2 was the principal component eluted from other Streptococci and A. viscosus. The MG2 which eluted from the surface of A. viscosus migrated with an electrophoretic mobility similar to asialo-MG2. These observations were verified by examining the interaction between 125I-HSMSL or 125I-HPS with several of the test strains. When 125I-salivary derived pellicles of S. sanguis were analyzed by SDS- PAGE/autoradiography, the autoradiographs were dominated by a component of approximately 55-60 kDa, as well as a low molecular weight band. The salivary derived pellicles from the other bacteria contained several other components of various molecular weights. These data indicate that selective interactions occur between the major salivary secretions and the surface of the bacterial strains tested. A manuscript summarizing these findings is in preparation. b. Characterization of the binding of parotid amylase (isoenzyme B1) to S. sanguis and other oral bacteria. Purified amylase (isoenzyme B1) was prepared from parotid saliva by gel- filtration chromatography, followed by FPLC anion-exchange chromatography. Purity was assessed by electrophoresis and amino-acid analysis. Experiments to determine the specificity of binding of 125I-labelled amylase B1 to S. sanguis and other oral bacteria are in progress.
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