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    Clinical study of the combined use of chemotherapy and rIL2(Biochemotherapy) in advanced patients with primary liver cancer and non small cell lung cancer
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    Study on Correlation between p53 Gene Deletion and Human Nonsmallcell Lung Cancer
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    Cell cycle analysis using flow cytometry displayed that transfection of FRNK gene decreased the cell number at S+G_2/M phase compared with the non transfected cells (P<0.05).
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The method applies to the standard arithmetic subgroups ofSO(n,1) (a case which was proved previously by Millson [Mi]), to the non-arithmetic lattices inSO(n,1) constructed by Gromov and Piatetski-Shapiro [GPS] and to groups generated by reflections.
      
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In the 3'-MeDAB induced liver tumour, it was found that the activities of glucoses-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase and dipeptidases were higher than those in the normal liver, while the activities of glutamic dehydrogenase, glutaminase(phosphate-activated), ornithine carbamyl transferase, tryptophan pyrrolase, threonine dehydrase and tyrosine transaminase were lower or even absent.Changes in most enzyme activities were observed in the precancerous stage and the pattern of these changes...

In the 3'-MeDAB induced liver tumour, it was found that the activities of glucoses-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase and dipeptidases were higher than those in the normal liver, while the activities of glutamic dehydrogenase, glutaminase(phosphate-activated), ornithine carbamyl transferase, tryptophan pyrrolase, threonine dehydrase and tyrosine transaminase were lower or even absent.Changes in most enzyme activities were observed in the precancerous stage and the pattern of these changes followed that in the liver tumour. Thus in the course of carcinogenesis, the activities of glucose-6-phosphate dehydrogenase, 6-phosphogluconic dehydrogenase and dipeptidase(glycylglycine as substrate)increased while those of glutamic dehydrogenase, glutaminase and ornithine carbamyl transferase decreased. However, there was no significant change in the activity of dipeptidase when DL-alanylglycine was used as substrate. Changes in activity of tryptophan pyrrolase and tyrosine transaminase were not pronounced as compared with those of the control. The activity of glutathione reductase in the liver tumour was similar to that of normal liver, but it increased from the 4th to 13th week of feeding of the carcinogen. Threonine dehydrase was remarkably influenced by the nutritive factor of the basal diet so that the effect of 3'-MeDAB on threonine dehydrase could not be observed during carcinogenesis.A comparative study has been made with 2-MeDAB, a non-carcinogenic substance. It had no apparent effect on the above enzymes except that it caused the activity of glutamic dehydrogenase to be higher than that of the control.Further experiments have shown that the specific activities of glutamic dehydrogenase and glutaminase in the mitochondria of liver tumour were lower than those of the control. In the precancerous liver the specific activity of glutaminase in the mitochondria was lower than that of the control, while there was no significant change in the case of glutamic dehydrogenase.From these results together with those from other laboratories a possible biochemical mechanism of the carcinogenesis induced by 3'-MeDAB was proposed(Fig. 12). It was suggested that the change in enzyme activity during carcinogenesis may possibly have resulted from the carcinogen being first metabolized in the liver, leading to a higher activity of the oxidative metabolism of glucose-6-phosphate and exhibiting influences on liver enzymes by the metabolites of 3'-MeDAB through different mechanisms. Consequently there produced an abnormal growth and differentiation of liver cell which became neoplastic with the formation of liver cancer, 2-MeDAB may be metabolized in a different way from that of 3'-MeDAB thus producing different effects on most enzyme activities. It is therefore evident that the specific effect of 3'-MeDAB on the liver enzymesmay be closely related to its property of carcinogenisity.

在3'-MeDAB誘发的肝癌組織中,G-6-PD、6-PGD、二肽酶的活性都較正常肝高,而另一些酶如GDH、GMA、OCT、TP、TD、TTA的活性則較正常肝低或甚至測不出来。大多数酶活性都在癌前期即有明显的变化,其变化情况多趋向于癌的特征,如肝癌組織中活性較高的酶,在引癌过程中其活性較对照組有升高趋势,如G-6-PD、6-PGD、二肽酶(以甘氨酰甘氨酸为底物);肝癌組織中活性降低的酶,在引癌过程中其活性有降低趋势,如GDH、GMA、OCT。但以丙氨酰甘氨酸为底物的二肽酶活性的变化則与对照組基本相似。癌前期TP及TTA活性較对照組都无明显差异。肝癌組織中GSSGR活性与正常肝相似,但在引癌过程中(4—13周)則有升高趋势。苏氨酸去水酶受基础食料中营养因素的影响較大,癌前期看不出3'-MeDAB对它的影响。非致癌物,2-MeDAB,除了使GDH活性升高外,对上述其他酶活性都无明显的影响。肝癌綫粒体內GMA和GDH比活性都較对照組及正常肝綫粒体为低。癌前期肝綫粒体GMA比活性較对照組显著降低,而GDH比活性則无明显改变。根据本实驗及其他实驗室結果,我們认为:3'-MeDAB所引起的肝脏酶活性变化,可能是由于它在肝...

在3'-MeDAB誘发的肝癌組織中,G-6-PD、6-PGD、二肽酶的活性都較正常肝高,而另一些酶如GDH、GMA、OCT、TP、TD、TTA的活性則較正常肝低或甚至測不出来。大多数酶活性都在癌前期即有明显的变化,其变化情况多趋向于癌的特征,如肝癌組織中活性較高的酶,在引癌过程中其活性較对照組有升高趋势,如G-6-PD、6-PGD、二肽酶(以甘氨酰甘氨酸为底物);肝癌組織中活性降低的酶,在引癌过程中其活性有降低趋势,如GDH、GMA、OCT。但以丙氨酰甘氨酸为底物的二肽酶活性的变化則与对照組基本相似。癌前期TP及TTA活性較对照組都无明显差异。肝癌組織中GSSGR活性与正常肝相似,但在引癌过程中(4—13周)則有升高趋势。苏氨酸去水酶受基础食料中营养因素的影响較大,癌前期看不出3'-MeDAB对它的影响。非致癌物,2-MeDAB,除了使GDH活性升高外,对上述其他酶活性都无明显的影响。肝癌綫粒体內GMA和GDH比活性都較对照組及正常肝綫粒体为低。癌前期肝綫粒体GMA比活性較对照組显著降低,而GDH比活性則无明显改变。根据本实驗及其他实驗室結果,我們认为:3'-MeDAB所引起的肝脏酶活性变化,可能是由于它在肝內进行代謝引起G-6-P旁路代謝的活跃,以及3'-MeDAB代謝产物通过各种不同机制对酶的影响所致。这些酶活性的变化可能导致肝細胞的异常生长和异常分化因而形成肝癌(图12)。非致癌物,2-MeDAB,可能与3'-MeDAB的代謝途径不同,因而产生不同的影响,而3'-MeDAB所产生的特殊影响則可能与其致癌作用有关。

(1) A comparative study has been made on the induction of tryptophan pyrrolase by substrate and corticoids in liver tumor and the precancerous liver induced by 3'-MeDAB.(2) The liver tumor, contrary to normal liver, was inactive in response to both tryptophan and hydrocortisone for the induction of tryptophan pyrrolase, while the tissue adjacent to the tumor was active with respect to both substrate and hormonal induction.(3) A decrease in both substrate and hormonal induction was observed in the precancerous...

(1) A comparative study has been made on the induction of tryptophan pyrrolase by substrate and corticoids in liver tumor and the precancerous liver induced by 3'-MeDAB.(2) The liver tumor, contrary to normal liver, was inactive in response to both tryptophan and hydrocortisone for the induction of tryptophan pyrrolase, while the tissue adjacent to the tumor was active with respect to both substrate and hormonal induction.(3) A decrease in both substrate and hormonal induction was observed in the precancerous liver developed by feeding 3'-MeDAB for different time intervals. In experiments by injecting intraperitoneally the carcinogen into animals,for 25 hours, similar results were obtained as in the feeding experiments.(4) 2-MeDAB, a non-carcinogenic substance, caused the same effect on the induction of tryptophan pyrrolase in every case as did 3'-MeDAB. It thus appears that the effect of 3'-MeDAB on the enzyme induction may not be specific.(5) No inhibitors of tryptophan pyrrolase or activators of kynureninase were found in the cell sap of liver tumor and the liver of rats fed 3'-MeDAB or 2-MeDAB in the course of induction.(6) The cell sap from liver tumor (non-induced) contained only a small amount of enzyme protein, as shown by the fact that the enzyme activity being only slightly increased by the addition of either normal microsome or hematin, of which the level has not elevated by the administration of tryptophan or hydrocortisone.(7) Similar experiments have shown that the cell sap from the substrate and hormonal induced liver in the precancerous stage contained a decreased amount of enzyme protein as compared to that of the control. The same was true of the rats fed 2-MeDAB.(8) Microsomes from liver tumor have lost almost completely the ability of activating tryptophan pyrrolase in the cell sap. The ability of activation due to microsomes from the precancerous liver was remarkably reduced, though not yet completely lost, while the microsomes from the liver of rats fed 2-MeDAB were normal. It was in this respect that the effect of non-carcinogen (2-MeDAB) was found to be different from that of the carcinogen (3'-MeDAB).(9) From the results presented, it was concluded that the default of tryptophan pyrrolase induction observed in the liver tumor and the precancerous liver was mainly due to an inadequate amount of apoenzyme, rather than a deficiency of co-factor (hematin) or an increment of protein other than the enzyme. The possible cause of these effects was briefly discussed.

本文对大鼠肝癌及癌前期肝内TP的底物诱导和激素诱导作了比较研究。在3′-MeDAB诱发的肝癌中,TP活性很低,且不因注射色氨酸或氢可地松而升高,而癌周组织则仍保留对底物和激素诱导的能力。喂3′-MeDAB 13天、28天、90天大鼠肝内TP的底物诱导效应都较对照组为低。急性注射3′-MeDAB25小时,以100毫克/100克体重的L-色氨酸进行诱导,TP的诱导效应亦较对照组为低。氢可地松诱导的结果与底物诱导的相似,无论在喂或急性注射3′-MeDAB的情况下,TP的诱导效应都受到抑制。但在相同条件下,非致癌物,2-MeDAB,对TP的底物诱导和激素诱导(慢性的或急性的实验)也有相似的作用。诱导后肝癌组织或喂偶氮染料的肝组织中都未发现有TP的抑制物或狗尿酸酶的激活物。微粒体及正铁血红素与上清液的加合实验表明:(1)肝癌微粒体几乎完全不具有激活TP的活力;癌前期(3′-MeDAB组)肝微粒体已部分失去此种生化功能,但2-MeDAB组微粒体则否。3′-MeDAB对肝微粒体中辅助因子(正铁血红素)的结构并无破坏,而可能使辅助因子的含量减少。(2)微粒体对激活上清液TP的效果较自由的正铁血红素差,即使加入过量微粒体亦不能...

本文对大鼠肝癌及癌前期肝内TP的底物诱导和激素诱导作了比较研究。在3′-MeDAB诱发的肝癌中,TP活性很低,且不因注射色氨酸或氢可地松而升高,而癌周组织则仍保留对底物和激素诱导的能力。喂3′-MeDAB 13天、28天、90天大鼠肝内TP的底物诱导效应都较对照组为低。急性注射3′-MeDAB25小时,以100毫克/100克体重的L-色氨酸进行诱导,TP的诱导效应亦较对照组为低。氢可地松诱导的结果与底物诱导的相似,无论在喂或急性注射3′-MeDAB的情况下,TP的诱导效应都受到抑制。但在相同条件下,非致癌物,2-MeDAB,对TP的底物诱导和激素诱导(慢性的或急性的实验)也有相似的作用。诱导后肝癌组织或喂偶氮染料的肝组织中都未发现有TP的抑制物或狗尿酸酶的激活物。微粒体及正铁血红素与上清液的加合实验表明:(1)肝癌微粒体几乎完全不具有激活TP的活力;癌前期(3′-MeDAB组)肝微粒体已部分失去此种生化功能,但2-MeDAB组微粒体则否。3′-MeDAB对肝微粒体中辅助因子(正铁血红素)的结构并无破坏,而可能使辅助因子的含量减少。(2)微粒体对激活上清液TP的效果较自由的正铁血红素差,即使加入过量微粒体亦不能使TP活性增高到加入正铁血红素的水平;微粒体对3′-MeDAB组上清液的激活不如对2-MeDAB组及对照组上清液(底物或激素诱导)的激活显著,而正铁血红素对三组上清液都有显著激活。(3)肝癌细胞上清液只合有极少量的TP蛋白,且不因注射色氨酸或氢可地松而增加;癌前期肝细胞上清液的TP蛋白因底物或激素诱导而增加的量都较对照粗低。2-MeDAB组也有相似现象。以上结果表明,肝癌及癌前期肝内TP诱导的受损,主要是由于诱导后TP蛋白的缺少,而不是由于辅助因子(如正铁血红素)的不足,或非酶蛋白的增多。

Transfer factor (TP) is a dialysable (ultrafilterable) extract of sensitised leukocytes. It transfers cellular immunity from a skin test positive donor to a skin test negative recipient. Currently TF is recognized as one of the most potent immunological reagents. In this paper the detailed method for preparation of transfer factor from normal blood bank donors has been described and some physico-chemical and biological properties of the TF preparations have been examined. The production of TF is briefly as follows:...

Transfer factor (TP) is a dialysable (ultrafilterable) extract of sensitised leukocytes. It transfers cellular immunity from a skin test positive donor to a skin test negative recipient. Currently TF is recognized as one of the most potent immunological reagents. In this paper the detailed method for preparation of transfer factor from normal blood bank donors has been described and some physico-chemical and biological properties of the TF preparations have been examined. The production of TF is briefly as follows: After separation of the plasma (for plasma products), the buffy coats are harvested and pooled. The contaiminating red blood cells are disrupted by tris buffered or isotonic NH_4Cl solution. The pooled leukocytes having been washed iwice with cold normal saline are then alternately frozen and thawed ten times with dry ice in acetone and a 37℃ water bath. The cell lysate is placed in dialysis tubing and dialysed in the cold for 36~48 hours against running pyrogenfree deionized water. The dialysate is lyophilized. The yellowish white powder is saved and redissolved in the desired volume of pyrogen-free deionized water, and passed through a Seitz filter (EKS). 2ml of the sterile TF solution (equivalent to the dialysate of 4×10~8 leukocytes) are placed in each ampoule. The final product is stored at -20℃.The TF preparation is protein-free as determined by protein precipitating reagents. It contains ca. 148μg of peptides and 14μg of ribose per mg of dry powder. The ultraviolet absorption curve gives a peak at 250~251nm. Adenine, guanine and uracil are present in the paper chromatogram of the TF acid hydrolysate. Silica- gel thin layer chromatography reveals four spots stained with ninhydrin. Sephadex G-25 filtration gives reproducibly a characteristic elution pattern yielding 3 main peaks and several small peaks with many of the eluted peaks beyond the total volume of the column. The results of animal experiments show that the TF preparations are non-toxic, non-anaphylactic and non-antigenic.So far over 160 patients (variously afflicted with herpes zoster, chronic hepatitis B, systemic lupus erythematosus, primary carcinoma of the liver, carcinoma of the lung and leukemia) have been treated with the TF preparations. The results will be published elsewhere.

转移因子是致敏白细胞中的可透析物质,能将一个有免疫能力的人的某些细胞免疫力转移给无免疫力的人。所以供给转移因子可能是一种有效的免疫治疗措施。本文详细介绍综合利用血源制备正常人转移因子的方法,并分析其某些理化性质和生物学性质。收集分离血浆后的白细胞层,用三羟甲基氨基甲烷缓冲的或等渗的氯化铵溶液破坏其中污染的红细胞,白细胞经生理盐水洗涤后进行10次冻融,白细胞匀浆对流动去离子水透析,透析液冷冻干燥、除菌分装。每安瓿2毫升转移因子注射液相当4×10~8个白细胞的透析物,保存于-20℃备用。本制剂蛋白质定性检查阴性;每毫克干粉约含多肽148微克、核糖14微克;在250~251毫微米有吸收高峰;转移因子酸水解液硷基纸层析有三种硷基;硅胶薄板层析呈四个茚三酮显色点;葡聚糖G-25凝胶过滤呈可重复的特征性洗脱图谱,具有3个主要峰及若干个小峰,主要洗脱部分在V_t之后。动物实验表明此制剂无毒性、无过敏性和抗原性。本制剂已用于临床治疗带状疱疹、系统性红斑狼疮、慢性乙型肝炎、原发性肝癌、肺癌及白血病等一百六十余例,结果将另文发表。

 
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