余甘子中抗坏血酸的差示分光光度测定法

本文采用差示分光光度法测定了余甘子果实中的抗坏血酸,方法简便、快速、重现性好、样品(?)试剂用量少,结果与药典的方法吻合。测定结果表明,四川省凉山地区的余甘子果实(?)抗坏血酸含量在0.88～2.4mg/g之间。     

特定电磁波对作物幼苗抗坏血酸过氧化物酶活性和谷胱甘肽含量的影响

特定电磁波辐射器辐照玉米、小麦、绿豆干种子及发芽种子后,加一定量水置２８℃恒温下培育,然后定期取样分析测定幼芽和幼苗中抗坏血酸过氧化物酶活力及ＧＳＨ和抗坏血酸含量。研究指出,特定电磁波显著提高了酶活力及上述两种生理活性物质含量,增加幅度为１２％－６８％。作者认为用特定电磁波辐照种发芽种子有助于提高作物幼苗的抗逆能力。     

低温胁迫对水稻幼苗抗坏血酸含量的影响

随着低温时间的延长,水稻幼苗抗坏血酸和GSH的含量均平行地下降,抗坏血酸含量与电解质渗出率之间呈负相关。增强低温胁迫程度,随着抗坏血酸含量逐渐减少,MDA含量则逐渐增加。经低温处理后在不同光强下恢复时,抗坏血酸和MDA含量的变化不同。抗氧化剂(GSH、半胱氨酸和巯基乙醇)的预处理可抑制低温引起的抗坏血酸含量的下降。     

CHLOROPHYLL-SENSITIZED REDUCTION OF PLASTOQUINONE BY ASCORBIC ACID AND QUENCHING OF CHLOROPHYLL-FLUORESCENCE BY PLASTOQUINONE

1. Photochemical reduction of plastoquinone by ascorbic acid inethanol was sensitized with some derivatives of chlorophyll.The order of effectiveness was as follows: allomerized chlorophylla > chlorophyllin a > chlorophyll a > chlorophyll b> pheophytin a.
2. Quenching of the fluorescence of chlorophylla by plastoquinonewas observed. The quenching constant calculatedwas 71 litreper mole.

¹Contribution No. 159 from the Department of Biology, Facultyof Science, Kyushu University. Supported in part by a grant-in-aidfor Fundamental Scientific Research from the Ministry of Education. ²Present address: Biological Laboratory, General Education Department,Kyushu University, Ropponmatsu, Fukuoka. ³Present address: Biological Institute, Daiichi College of PharmaceuticalSciences, Tamagawa-machi, Takamiya, Fukuoka.     

高效毛细管电泳法测定甘草中甘草酸的含量

采用高效毛细管电泳法成功地分离测定了甘草中甘草酸的含量, 在pH=5.8 的50mmol/L 磷酸缓冲液, 检测波长252nm, 分离电压25KV, 进样压力20 mm 汞柱, 温度30℃的检测条件下, 标准溶液在0.0448mg/ml~0.224mg/ml 范围内与峰面积成良好的线性关系, 回归方程为:Y=4.16×10⁶x-8.94×10⁴, 相关系数r=0.9939, 具有较高的灵敏度和准确度。该法操作简便、迅速、可靠、测试费用低。     

THE PREPARATION AND PROPERTIES OF HIGHLY PURIFIED ASCORBIC ACID OXIDASE

1. A method is described for the preparation of a highly purified ascorbic acid oxidase containing 0.24 per cent copper. 2. Using comparable activity measurements, this oxidase is about one and a half times as active on a dry weight basis as the hitherto most highly purified preparation described by Lovett-Janison and Nelson. The latter contained 0.15 per cent copper. 3. The oxidase activity is proportional to the copper content and the proportionality factor is the same as that reported by Lovett-Janison and Nelson. 4. When dialyzed free of salt, the blue concentrated oxidase solutions precipitate a dark green-blue protein which carries the activity. This may be prevented by keeping the concentrated solutions about 0.1 M in Na₂HPO₄. 5. When highly diluted for activity measurements the oxidase rapidly loses activity (irreversibly) previous to the measurement, unless the dilution is made with a dilute inert protein (gelatin) solution. Therefore activity values obtained using such gelatin-stabilized dilute solutions of the oxidase run considerably higher than values obtained by the Lovett-Janison and Nelson technique. 6. The effect of pH and substrate concentration on the activity of the purified oxidase in the presence and absence of inert protein was studied.