缅怀与思念——记谈家桢院士对我国生物技术的贡献

我国现代遗传学奠基人、杰出的遗传学家谈家桢先生走完了百年的光辉历程,他的毕生事业和高尚品格将永远活在我们心中!     

智者魅力 学界楷模——记著名遗传学家谈家桢

谈家桢先生是我国著名的遗传学家,也是中国遗传学的奠基人之一。自从谈先生1930年进入燕京大学师从李汝祺教授研究遗传学以来,他始终活跃在遗传学研究及教学的最前沿,并致力于促进中国遗传学与世界的交流,为中国乃至世界遗传学事业的发展做出了巨大贡献。今年恰逢谈先生的百岁华诞,《生命世界》特别邀请全国政协委员、《谈家桢与遗传学》一书的作者赵功民先生为本刊撰文,以示对这位杰出科学家百岁寿辰的祝贺。     

纪念著名遗传学家谈家桢先生诞辰110周年

<正>2019年是谈家桢先生诞辰110周年。谈先生是国际著名遗传学家、中国现代遗传学奠基人之一,为中国遗传学的发展做出了杰出贡献。谈先生1909年9月15日出生于浙江宁波,本科毕业于东吴大学,硕士毕业于燕京大学,1936年于美国加州理工学院的摩尔根实验室获得博士学位。谈先生于1937年回国后被聘为浙江大学教授,1952年被聘为复旦大学     

我国医学遗传学奠基人之一——罗会元教授

正罗会元是我国医学遗传学奠基人之一,著名医学遗传学家,中国医学科学院基础医学研究所、北京协和医学院医学遗传学教授,博士生导师。1946年至1951年就读于Johns Hopkins医学院,获医学博士。1955年毅然回国,在他所钟情的北京协和医学院从事医疗、科研和教学半个多世纪。因在医学遗传学教学和国际交流中的杰出贡献,1999年获Johns Hopkins医学院国际教育成就奖。历任中     

著名细胞生物学家施履吉

<正>施履吉先生是我国著名的细胞生物学家和遗传学家。1917年11月26日生于江苏仪征,6岁丧父,由母亲教养成人。1935年,他从上海惠平中学毕业,考入浙江大学园艺系,后因意识到"吃饭问题"对于当时中国的重要性,便由园艺专业改读了育种专业。1941年,考入浙江大学理科研究院,师从谈家桢教授攻读细胞遗传学。     

纪念卓越的生理学家林可胜教授

林可胜教授(1897～1969)是我国现代生理学的奠基人。他在消化生理学和痛觉生理学两方面都是先驱,曾获得国际声誉。他是一位卓越的生理学家。生平事迹林可胜教授祖籍福建厦门,1897年10月15日生于新加坡。其父林文庆曾受奖学金资助,赴英国爱丁堡大学学医,学成归国后,曾任孙中山先生的机要秘书和随身医生,后任厦门大学校长。林可胜教授于8岁时,即被送至英国爱丁堡读书,1919年毕业于爱丁堡大学医学院,翌年又获哲学博士学位。他的导师是著名的生理学家沙佩-谢佛(Shar-poy-Schafer)教授,对他深为器重,曾聘他担任讲师职位。1923年他当选为英国皇家学会爱丁堡     

生命科学和医学学部2013年当选院士简介

金力 进化遗传学家。复旦大学教授。1963年3月13日出生于上海市,籍贯浙江上虞。1985年毕业于复旦大学,1987年获该校硕士学位,1994年在美国德克萨斯大学获博士学位。现任复旦大学副校长。     

怀念导师陈桢先生

时光飞驰,瞬眼间陈桢导师逝世已六年了。在党和国家大力发展科学研究事业的今日,更使我们怀念我国动物遗传学的奠基人——陈桢导师。虽然他和我们相处的时间不长,但却给我们留下了极为深刻的印象,久久不能忘怀。陈桢先生的学识渊博,在生物科学的很多方面都     

复旦国际遗传学新前沿讨论会

复旦国际遗传学新前沿讨论会将于1989年9月10日到13日在上海宝隆宾馆召开。会议的主要目的是为促进我国遗传学的发展和加强国际间的交流和合作;建立复旦大学T.H.摩尔根科学中心;表扬谈家桢教授从事遗传学教学和科研工作六十年,同时祝贺他的八十寿辰。本次国际会议的主要议题有四个:(1)果蝇遗传学的最新进展,(2)人类遗传学新进     

我国现代生理学的奠基人——林可胜

林可胜教授(1897—1969)是一位卓越的生理学家,是我国现代生理学的奠基人。林教授祖籍福建省厦门市,1897年10月15日生于新加坡。1919年毕业于爱丁堡大学医学院,翌年获哲学博士学位。1925年秋,林可胜回国就任北京协和医学院生理系主任教授,一直工作了十二年。1949年,他离华赴美先后进行消化生理学和痛觉生理与镇痛药物的研究。1969年7月8日因患食道癌在拉丁美洲的牙买加逝世。林可胜教授是我国现代生理学的奠基人,为我国生理学的发展作出了巨大的贡献。1926     

Complement components C5 and C7: recombinant factor I modules of C7 bind to the C345C domain of C5

Studies reported over 30 years ago revealed that latent, nonactivated C5 binds specifically and reversibly to C6 and C7. These reversible reactions are distinct from the essentially nonreversible associations with activated C5b that occur during assembly of the membrane attack complex, but they likely involve some, perhaps many, of the same molecular contacts. We recently reported that these reversible reactions are mediated by the C345C (NTR) domain at the C terminus of the C5 alpha-chain. Earlier work by others localized the complementary binding sites to a tryptic fragment of C6 composed entirely of two adjacent factor I modules (FIMs), and to a larger fragment of C7 composed of its homologous FIMs as well as two adjoining short consensus repeat modules. In this work, we expressed the tandem FIMs from C7 in bacteria. The mobility on SDS-polyacrylamide gels, lack of free sulfhydryl groups, and atypical circular dichroism spectrum of the recombinant product rC7-FIMs were all consistent with a native structure. Using surface plasmon resonance, we found that rC7-FIMs binds specifically to both C5 and the rC5-C345C domain with K(D) approximately 50 nM, and competes with C7 for binding to C5, as expected for an active domain. These results indicate that, like C6, the FIMs alone in C7 mediate reversible binding to C5. Based on available evidence, we suggest a model for an irreversible membrane attack complex assembly in which the C7 FIMs, but not those in C6, are bound to the C345C domain of C5 within the fully assembled complex.     

Co-function of C3-and C4-photosynthetic pathways in C3, C4 and C3-C4 intermediate Flaveria species

The potential for C₄ photosynthesis was investigated in five C₃-C₄ intermediate species, one C₃ species, and one C₄ species in the genus Flaveria, using ¹⁴CO₂ pulse-¹²CO₂ chase techniques and quantum-yield measurements. All five intermediate species were capable of incorporating ¹⁴CO₂ into the C₄ acids malate and aspartate, following an 8-s pulse. The proportion of ¹⁴C label in these C₄ products ranged from 50–55% to 20–26% in the C₃-C₄ intermediates F. floridana Johnston and F. linearis Lag. respectively. All of the intermediate species incorporated as much, or more, ¹⁴CO₂ into aspartate as into malate. Generally, about 5–15% of the initial label in these species appeared as other organic acids. There was variation in the capacity for C₄ photosynthesis among the intermediate species based on the apparent rate of conversion of ¹⁴C label from the C₄ cycle to the C₃ cycle. In intermediate species such as F. pubescens Rydb., F. ramosissima Klatt., and F. floridana we observed a substantial decrease in label of C₄-cycle products and an increase in percentage label in C₃-cycle products during chase periods with ¹²CO₂, although the rate of change was slower than in the C₄ species, F. palmeri. In these C₃-C₄ intermediates both sucrose and fumarate were predominant products after a 20-min chase period. In the C₃-C₄ intermediates, F. anomala Robinson and f. linearis we observed no significant decrease in the label of C₄-cycle products during a 3-min chase period and a slow turnover during a 20-min chase, indicating a lower level of functional integration between the C₄ and C₃ cycles in these species, relative to the other intermediates. Although F. cronquistii Powell was previously identified as a C₃ species, 7–18% of the initial label was in malate+aspartate. However, only 40–50% of this label was in the C-4 position, indicating C₄-acid formation as secondary products of photosynthesis in F. cronquistii. In 21% O₂, the absorbed quantum yields for CO₂ uptake (in mol CO₂·[mol quanta]^-1) averaged 0.053 in F. cronquistii (C₃), 0.051 in F. trinervia (Spreng.) Mohr (C₄), 0.052 in F. ramosissima (C₃-C₄), 0.051 in F. anomala (C₃-C₄), 0.050 in F. linearis (C₃-C₄), 0.046 in F. floridana (C₃-C₄), and 0.044 in F. pubescens (C₃-C₄). In 2% O₂ an enhancement of the quantum yield was observed in all of the C₃-C₄ intermediate species, ranging from 21% in F. ramosissima to 43% in F. pubescens. In all intermediates the quantum yields in 2% O₂ were intermediate in value to the C₃ and C₄ species, indicating a co-function of the C₃ and C₄ cycles in CO₂ assimilation. The low quantum-yield values for F. pubescens and F. floridana in 21% O₂ presumably reflect an ineffcient transfer of carbon from the C₄ to the C₃ cycle. The response of the quantum yield to four increasing O₂ concentrations (2–35%) showed lower levels of O₂ inhibition in the C₃-C₄ intermediate F. ramosissima, relative to the C₃ species. This indicates that the co-function of the C₃ and C₄ cycles in this intermediate species leads to an increased CO₂ concentration at the site of ribulose-1,5-bisphosphate carboxylase/oxygenase and a concomitant decrease in the competitive inhibition by O₂.Abbreviations PEP phosphoenolpyruvate - PGA 3-phosphoglycerate - RuBP ribulose-1,5-bisphosphate     

Human C4 haplotypes with duplicated C4A or C4B

In the course of study of families for the sixth chromosome markers HLA-A, C, B, D/DR, BF, and C2, the two loci for C4, C4A, and C4B, and glyoxalase I, we encountered five examples of probable duplication of one or the other of the two loci for C4. In one of these, both parents and one sib expressed two different structural genes for C4B, one sib expressed one, and one sib expressed none, suggesting that two C4B alleles were carried on a single haplotype: HLA-A2, B7, DR3, BFS1, C2C, C4A2, C4B1, C4B2, GLO1. In a second case, two siblings inherited C4B*1 and C4B*2 from one parent and C4B*Q0 from the other. This duplication appeared on the chromosome as HLA-AW33, B14, DR1, BFS, C2C, C4A2, C4B1, C4B2, GLO2. In a third, very large family with 3 generations, a duplication of the C4B locus occurred which was followed in 2 generations. In one individual, there were three C4B alleles and two C4A alleles. One of the C4B alleles had a hemolytically active product with electrophoretic mobility near C4B2 and was designated C4B*22. It segregated with C4B1 in the family studied. The complete haplotype was HLA-A11, CW1, BW56, DR5, BFS, C2C, C4A3, C4B22, C4B1, GLO2. In another family with 12 siblings, one parent and eight children expressed two C4A alleles on the haplotype HLA-AW30, BW38, DR1, BFF, C2C, C4A3, C4A2, C4BQ0, GLO1.(ABSTRACT TRUNCATED AT 250 WORDS)     

Expression and characterization of the C345C/NTR domains of complement components C3 and C5

Complement components C3, C4, and C5 are members of the thioester-containing alpha-macroglobulin protein superfamily. Within this superfamily, a unique feature of the complement proteins is a 150-residue-long C-terminal extension of their alpha-subunits that harbors three internal disulfide bonds. Previous reports have suggested that this is an independent structural module, homologous to modules found in other proteins, including netrins and tissue inhibitors of metalloproteinases. Because of its distribution, this putative module has been named both C345C and NTR. To assess the structures of these segments of the complement proteins, their relationships with other domains, and activities as independent structures, we expressed C345C from C3 and C5 in a bacterial strain that permits cytoplasmic disulfide bond formation. Affinity purification directly from cell lysates yielded recombinant C3- and C5-C345C with properties consistent with multiple intramolecular disulfide bonds and high beta-sheet contents. rC5-, but not rC3-C345C inhibited complement hemolytic activity, and surface plasmon resonance studies revealed that rC5-C345C binds to complement components C6 and C7 with dissociation constants of 10 and 3 nM, respectively. Our results provide strong evidence that this binding corresponds to the previously described reversible binding of C5 to C6 and C7, and taken together with earlier work, indicate that the C5-C345C module interacts directly with the factor I modules in C6 and C7. The high binding affinities suggest that complexes composed of C5 bound to C6 or C7 exist in plasma before activation and may facilitate assembly of the complement membrane attack complex.