Characterization of purified cytochrome b-c1 complex from Rhodopseudomonas sphaeroides R-26

A highly purified cytochrome b-c1 complex from Rhodopseudomonas sphaeroides R-26 was isolated by a procedure involving Triton X-100 solubilization, calcium phosphate column chromatography, and ammonium sulfate fractionation. The purified enzyme complex contains, in nanomoles/mg of protein, cytochrome b, 8.3; cytochrome c1, 8.3; iron-sulfur protein, 15; phospholipids, 182; and ubiquinone, 5. Four major polypeptides with apparent molecular weights of 48,000, 30,000, 24,000, and 12,000 were detected in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The Mr = 48,000 and 30,000 proteins are cytochromes b and c1, respectively. The enzyme complex catalyzes electron transfer from ubiquinol to cytochrome c with a specific activity of 12.6 mumol of cytochrome c reduced per min/mg of protein at 23 degrees C. This is lower than that of the mitochondrial enzyme, although both systems have similar essential redox components and a similar Km for ubiquinol. The activity is fully sensitive to antimycin A and 5-n-undecyl-6-hydroxy-4, 7-dioxobenzothiazole. The enzyme complex is stable at neutral pH and at lower temperatures, but became less stable when the incubation temperature was raised. At 37 degrees C, the half-life is 15 min. The enzymatic activity was insensitive to treatment with N',N'-dicyclohexylcarbodiimide. No p-chloromercuriphenylsulfonate-alkylable sulfhydryl groups were detected. The major phospholipids associated with the purified enzyme complex are phosphatidylcholine, phosphatidylethanolamine, and phosphatidylglycerol with molar per cent distributions of 25, 21, and 35, respectively. About 60% of the enzymatic activity was abolished upon treatment with phospholipase A2. The phospholipase A2-inactivated activity can be partially restored by the addition of EDTA followed with phospholipids prepared from either the cytochrome b-c1 complex of the same source or a mixture of phosphatidylglycerol and asolectin.(ABSTRACT TRUNCATED AT 250 WORDS)     

青枯假单胞杆菌噬菌体ZP-2和ZP-3的生物学性状

噬菌体可作为检测和区分植物病原细菌的一种手段。有关青枯假单胞杆菌(Pseudomo-n~(as solanacearum) 噬菌体的研究工作报道不多,姜瘟菌株上的噬菌体则还未见报道。本文所报道的关于分离自土壤的青枯假单胞杆菌姜瘟菌株(ZO-12)的噬菌体ZP-2和ZP-3生物学性状的研究结果,可为这些噬菌体的利用提供参考依据。     

赤霉素产生菌~#85104菌株原生质体的形成再生和紫外光对原生质体诱变条件的研究

赤霉产生菌在正常条件下不产生孢子,育种材料以多核菌丝体及其碎片为主,大部分常用的诱变剂对它们诱变效应较差。本文报导有关赤霉素产生菌~#85104菌株原生质体的获得、再生和紫外光诱变原生质体的条件,甘氨酸对菌丝体生长的影响,以及采用二硫苏糖醇预处理菌丝体等方面条件的研究。在采用紫外光照射原生质体的诱变处理下,已获得数株高产的新菌株。     

水稻叶片衰老过程中氨肽酶活性的变化

水稻叶片中存在着氨肽酶,其最适反应pH和最适反应温度分别为8.2℃和40℃,酶促反应的产物量在最初30min内与时间呈直线相关。 水稻叶片衰老过程中叶绿素和蛋白质含量下降,而氨肽酶比活上升;用植物激素延缓或促进叶片衰老蛋白质降解的同时也抑制或促进了氨肽酶比活的上升,说明氨肽酶在水稻叶片衰老蛋白质降解过程中起一定的作用。根据水稻叶片衰老过程中大分子化合物和叶片外部形态的变化,可将叶片衰老过程划分为缓衰期、急衰期和竭衰期。     

庐山蛾类区系研究

庐山,地处中亚热带北沿,北纬29.35°,东经115.59°,属亚热带东部季风区域。庐山襟江带湖,雨量充沛,植物种类繁多,种子植物有1800余种,隶属158科642属。因此,庐山蛾类也较丰富。笔者于1975年5月开始,对庐山蛾类进行了调查,共鉴定出蛾类455种。现将庐山蛾类区系报告如下。 区系分析 庐山蛾类已鉴定出32科340届455种。区系情况如表。 从表可以看出:     

Systematics ofNama (Hydrophyllaceae): Flavonoids and phyletic position of sect.Arachnoidea and sect.Cinerascentia

Eight flavonoids, four 6-oxygenated flavones, two methyl ethers of luteolin, apigenin 6,8-C-diglucoside and quercetin 3-O-glucoside, were isolated fromNama lobbii andN. rothrockii, sole members of sects.Arachnoidea andCinerascentia, respectively. Both taxa diverge markedly from other namas in morphology and chromosome number and their placement inNama has been questioned. The occurrence of 6-oxygenated flavones in these taxa adds to their already distinctive nature. Flavonoid evidence argues that both are more closely allied toEriodictyon than either is toNama.     

Cytochrome c in Hydrogenomonas eutropha

A c-type cytochrome from Hydrogenomonas eutropha was purified 150-fold by butanol extraction, ammonium sulfate precipitation, and column chromatography. Three distinct c-type cytochromes were recovered which did not bind with either carbon monoxide or cyanide and hence did not appear to be denatured. Polyacrylamide gel electrophoresis indicated that one protein was acidic and the other two were basic. The acidic cytochrome c had a sedimentation coefficient of 3.46. Its amino acid composition was not markedly different from other bacterial cytochromes, but relative to mammalian cytochromes c it was low in lysine, threonine, and isoleucine and high in alanine and valine.     

胎盘型碱性磷酸酶的纯化及部分性质的研究

 <正> 胎盘型碱性磷酸酶(P-ALP)是碱性磷酸酶(EC3.1.3.1.ALP)的一种同工酶。P-ALP除出现于妊娠妇女血清外,一些学者还从恶性肿瘤患者血清中发现此酶,并证明它是一种特异性较强的肿瘤标志物。据此,建立P-ALP的简易纯化方法,制备纯度较高的酶制品是建立P-ALP灵敏的微量检测法的先决条件。本文报道以L-苯丙氨酸(L-phe)为配基,用氯代环氧丙烷活化Sepharose 4B的亲和层析法,从人胎盘纯化P-ALP,并对其部分性质进行了研究。