Studies Concerning Affinity

نویسنده

  • P. Waage
چکیده

This article presents an English translation of "Studies Concerning Affinity" ( I ) , Guldherg and Waage's first presentation, in 1864, of the law of mass action. The source of this translation is a facsimile of the Norwegian original that appeared in 1964 as part of the proceedings of a symposium (2) commemorating the centennial of the law of mass action. Unfortunately, the figures displaying the experimental data presented in 1864 no longer exist (3) and do not appear in the 1964 facsimile. This lecture to the Academy of Sciences in Christiania (Oslo) was followed by twoothers in 1864, "Experiments for Determining the Affinity Law" (4) and "Concerning the Laws of Chemical Affinity" (5). In order to expand their potential audience, Guldberg and Waage puhlished a pamphlet in French, "Studies in Chemical Affinity" (6) , in 1867. A German paper, "Concerning Chemical Affinity" (7), in 1879 concluded their publications on chemical equilibrium. Although, except for the last publication, these writings are not readily available in American libraries, Ahegg's German translations in "Ostwald's Klassiker der Exakten Wissenschaft" (8) offer some access to most of them. These include excerpts from the lecture translated in this article and the third 1864 lecture as well as the entire French pamphlet of 1867. Abegg also provides a reprint, with commentary, of the 1879 journal article. An English translation of a portion of the introduction to this article appears in "A Source Book in Chemistry, 1400-1900" (9). The following translation tries to stay as close as possible to the st& of the orieinal. Canseauentlv. it oresen& substances bv ~ ~~ 4~~ . ~ .. . Rneliah names in m e in 18fi4. Brackets containing the modern .-.... ~~~~-~~~ -.. -~~~ ~ ~ ~~~ ~~~

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Development of aptameric affinity ligands specific to human plasma coagulation factor VIII using SEC-SELEX

Protein specific aptamers are highly applicable affinity ligands in different fields of research and clinical applications. They have been developed against various targets, in particular, bio-macromolecules such as proteins. Among human proteins, the coagulation factors are the most attractive targets for aptamer selection and their specific aptamers had valuable characteristics in therapeutic...

متن کامل

Gateway-compatible vectors for plant functional genomics and proteomics.

Gateway cloning technology facilitates high-throughput cloning of target sequences by making use of the bacteriophage lambda site-specific recombination system. Target sequences are first captured in a commercially available "entry vector" and are then recombined into various "destination vectors" for expression in different experimental organisms. Gateway technology has been embraced by a numb...

متن کامل

Development of aptameric affinity ligands specific to human plasma coagulation factor VIII using SEC-SELEX

Protein specific aptamers are highly applicable affinity ligands in different fields of research and clinical applications. They have been developed against various targets, in particular, bio-macromolecules such as proteins. Among human proteins, the coagulation factors are the most attractive targets for aptamer selection and their specific aptamers had valuable characteristics in therapeutic...

متن کامل

Single Step Purification of Novel Thermostable and Chelator Resistant Amylase from Bacillus Licheniformis RM44 by Affinity Chromatography

Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...

متن کامل

Single Step Purification of Novel Thermostable and Chelator Resistant Amylase from Bacillus Licheniformis RM44 by Affinity Chromatography

Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005