in order to better guide those entering the field of the PCR, a better classification of the abstracts or even an index would have been help- ful. M Crasnier Coenzymes and Cofactors: Glutathione, vol 3, part A, XII + 930 p, £ 88.15; part B, XII + 848 p, £96.85, edited by D Dolphin, R Poui- son, O Avramovi6. 1989. Wiley Interscience Glutathione (GSH) and its disulfide (GSSG) together fulfill a myriad of vital roles in cells at all evolutionary stages. For example, GSH participates in several types of enzyme-catalyzed reactions as co- enzyme (eg, formaldehyde dehydrogenase) or cosubstrate (eg, glutathione peroxydase, glyoxalase I...). It is also crucial to a variety of life processes (maintenance of the -SH levels of proteins, di- sulfide exchange processes, removal of hydrogen peroxide, organic peroxides, protection against many toxic substances including heavy metals, various electrophiles and free radicals (including those derived from oxygen)). It is involved in inflammation and related processes by virtue of its contribution to leukotriene structure, in blood platelet function, calcium metabolism, pigmentation and membrane func- tion. This volume is divided into 2 parts, A and B, covering the chemis- try, biochemistry, medical and nutritional aspects of glutathione. Part A has chapters on the history, chemical and physical properties of glutathione as well as chapters related to synthesis, NMR studies and metabolism of glutathione. Three chapters cover the industrial production and applications of glraathione and related compounds. The enzyme systems in which glt~tathione functions as a cosubstrate or a eoenzyme are also covered. Part B contains chapters on pharmacological, toxicological and nutritional aspects of glutathione, the influence of glutathione on membranes and the relationship between glutathione and lipid peroxidation. Other roles of glutathione are also covered, such as metabolism of calcium, leukotriene biosynthesis, melanins and pigmentation and its action in pesticide metabolism. This volume is very important. It gives a synthetic overview of glutathione metabolism and function in microorganisms, plants or animals. A summary (conclusion and perspectives) is included at the end of almost every chapter. The bibliography references are up-to- date and abundant. The authors and subject indexes are exhaustive which is an important advantage. The figures, tables and text are clear and easy to read. In conclusion, this vdume should be a reference for microbiolo- gists, biochemists and those involved in the medical field. As noted by the editors, Coenzymes and Cofactors will serve as a companion series to The Enzymes and Methods in Enzymology. P Marli/:re Lectins, edited by N Sharon, H Lis. Chapman and Hall, 1989, pp 133, DM 19.50 "Leetins" by Sharon and Lis is a most appealing small volume which in a little more than 100 pages succeeds in describing the molecular 305 and biological properties of lectins, discussing their possible roles and listing their numerous applications in biology and biomedical research. It is not an exhaustive review of all that has ever been published about these fascinating proteins assembled under a single term because they all bind sugars. Such a review cannot be written simply because over 2000 articles are now published yearly concerning lectins. This is a book which one reads i about 2 hours and which imme- diately stimulates the reader into I~ ~king for specific applications for his / her own field of interest. An interesting historical introdu :tion with actual pictures of the pioneers in lectin research whets on ~'s appetite for what is to follow: a very well presented menu of all ,hat lectins have to offer to the modern biochemist: a wide spread t*~corrence, ~,variety of biological activities, a diversity of carbohydrate' s.aecificities, well defined struc- tural subfamilies, and finally, a large variety of applications (remem- ber ttae iamous book "Co,~.~,avalin A as a too!"% ~ Nathan Sharon and Halina Lis are themselves l~roeminent resear- chers in the field of lectins: they have publishe6 numerous papers about these proteins, have organized well-attended meetings and courses on the subject, and have been untiring promotors of research on these exciting proteins. This is why after completing the book one remains frustated about the single most intriguing issue confronting researchers in this field: what is the real function of lectins, wherever they are found? Sharon and Lis do discuss a variety of possibilities but do not come out strongly for any of them. Tiffs is a true challenge for today's lectinologist. A Strosberg Synchrotron Radiation in Structural Biolo~,, edited by RM Sweet, AD Woodhead. Plenum Publishing Corp, 1989, pp 371, vol 51, US $ 69.50 ~ .... I..~* . . . . . ,~:~*:~ :~ S:~. ~ : ~ ~., :~I. . . . . . . I ~ . . . . ~'~ oyu~m~.~,n ~,~.au~,n .~ n~n~ ~.nx~ ~y ~u-~n~y ~.~-~..~ m storag~ rings. [t cove~ a wid~ range of wavelengths and is espe~ly use~l in the far UV and X-ray range~ where synchrotron sources ~e much bfi~ter th~ cl~ic~ ones. X-rays ~d ~ G~t ~om s ~ trons is available at a dozen sites in the world. It has a histo~ of more than 15 y~ars in Hamburg, Orsay and Stanford, wh~re machi- nes built by panicle physicists [or ~lliding b¢~ ex~dmen~ have been dive~ed towards light production, fu recent years, larg~ sto- rage rings have been built for the ~le pu~ose of producing UV ~d X-ray light in England, Japan and the US. In France, t~s is the ~se of Super ACO in Orsay for UV and to the European proje~ ES~ in Grenoble for X-rays. From the sta~, st~ctural biologists have be~n ma~or users of the intense and highly-collimated X-ray beams emitted by synchrotron sources. Meetings have been devoted to biolo~cai applications of s~chrotron radiation, the mint re, at of w~ch is ~e S~ium which took place in 1988 at NSLS, the American faolity for X-ray production in Btookhaven, New York. ~me 30 pa~ were pr~nt~ at the Symposium. ~ey are now collected in a volume edited by RM Sweet and AV Woodhead ~om NS~. It reflects the general orientation of the S~mposium towards the technolo~ of s~chr~ tron radiation applied to protein c~stallography and spectroscopy. Hence, it will be useful to potential users who need to know about existing facilities and applications, but a detailed de~fiption of results should be sought dsewhere. A section is devoted to the description of major ex~fiment~ fa~- lities available in the US (CHESS at Comell U~ve~i~, SS~ in Stanford, NSLS in Brookhaven), Europe (LURE in O~ay, the