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蛋白质生物功能的探索2025|PDF|Epub|mobi|kindle电子书版本百度云盘下载
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- 邹承鲁著 著
- 出版社: 石家庄:河北教育出版社
- ISBN:7543450321
- 出版时间:2003
- 标注页数:444页
- 文件大小:20MB
- 文件页数:463页
- 主题词:
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图书目录
学术思想3
思维形成3
对生物学发展前瞻的看法5
再论科学研究道德问题7
正确评价基础研究成果13
我国基础研究面临的问题及一些建议20
发表科学论文要遵循国际惯例24
学术论文33
CYTOCHROME C MODIFIED BY DIGESTION WITH PEPSIN33
EXOGENOUS AND ENDOGENOUS CYTOCHROME C37
辅酶细胞色素还原酶系的研究 Ⅰ还原辅酶Ⅰ与琥珀酸的同时氧化54
琥珀酸脱氢酶的研究 Ⅰ分离、提纯及性质75
THE TRIPHASIC REDUCTION OF CYTOCHROME B IN THE SUCCINATE-CYTOCHROME C REDUCTASE93
从胰岛素A及B链重合成胰岛素101
INTERACTION AND RECONSTITUTION OF CARBOXYL-TERMINAL-SHORTENED B CHAINS WITH THE INTACT A CHAIN OF INSULIN119
FORMATION OF NATIVE INSULIN FROM THE SCRAMBLED MOLECULE BY PROTEIN DISULFIDE-ISOMERASE134
THE INSULIN A AND B CHAINS CONTAIN SUFFICIENT STRUCTURAL INFORMATION TO FORM THE NATIVE MOLECULE146
蛋白质功能基团的改变与其生物活力的关系 Ⅰ 用图解法求必需基团数并判断其性质153
蛋白质功能基团的改变与其生物活力的关系 Ⅱ 胰蛋白酶的必需硫硫键数目172
FORMATION OF A NEW FLUOROPHORE ON IRRADIATION OF CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE179
FORMATION OF ENZYME-SUBSTRATE DISULFIDE LINKAGE DURING CATALYSIS BY PROTEIN DISULFIDE ISOMERASE184
酶活性不可逆改变的动力学 Ⅰ 底物影响酶与抑制剂结合速度的动力学方程189
DETERMINATION OF THE RATE CONSTANT OF ENZYME MODIFICATION BY MEASURING THE SUBSTRATE REACTION IN THE PRESENCE OF THE MODIFIER204
KINETICS OF SUBSTRATE REACTION DURING IRREVERSIBLE MODIFICATION OF ENZYME ACTIVITY219
KINETICS OF INACTIVATION OF CREATINE KINASE DURING MODIFICATION OF ITS THIOL GROUPS268
KINETICS OF TRYPSIN INHIBITION BY ITS SPECIFIC INHIBITORS286
A COMPARISON OF ZN(Ⅱ)AND CO(Ⅱ)IN KINETICS OF INACTIVATION OF AMINOACYLASE BY 1,10-PHENANTHROLINE AND RECONSTITUTION OF THE APOENZYME305
COMPARISON OF THE RATES OF INACTIVATION AND CONFORMATIONAL CHANGES OF CREATINE KINASE DURING UREA DENATURATION323
LOCATION OF THE ACTIVE SITES OF SOME ENZYMES IN LIMITED AND FLEXIBLE MOLECULAR REGIONS338
CORMPARISON OF THE ACTIVITY AND CONFORMATION CHANGES OF LACTATE DEHYDROGENASE H4 DURING DENATURATION BY GUANIDINIUM CHLORIDE347
CONFORMATIONAL CHANGES AT THE ACTIVE SITE OF CREATINE KINASE AT LOW CONCENTRATIONS OF GUANIDINIUM CHLORIDE360
CONFORMATIONAL FLEXIBILITY OF ENZYME NACTIVE SITES375
ACTIVATION OF CHICKEN LIVER DIHYDROFOLATE REDUCTASE BY UREA AND GUANIDINE HYDROCHLORIDE IS ACCOMPANIED BY CONFORMATIONAL CHANGE AT THE ACTIVE SITE380
FOLDING OF THE NASCENT PEPTIDE CHAIN INTO A BIOLOGICALLY ACTIVE PROTEIN398
PROTEIN DISULFIDE ISOMERASE IS BOTH AN ENZYME AND A CHAPERONE410
CHAPERONE-LIKE ACTIVITY OF PROTEIN DISULFIDE ISOMERASE IN THE REFOLDING OF A PROTEIN WITH NO DISULFIDE BONDS418
附录427
一、著译要目427
二、学术活动大事记444
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