diately visible changes in plants dur­ing development and maturation in the greenhouse or field," according to a manuscript prepared by Green. He also notes: "Kernel weight, total protein, and threonine content of protein were not altered appreciably." Thus, the genetic change apparently affects the amounts of free threonine in the plant cell, without changing other proteins there.

That finding may take on added significance when weighed against recent findings about major storage proteins in corn kernels from research done by two other members of this Minnesota consortium, Irwin Ru-benstein of the department of genet­ics and cell biology, and Joachim Messing of the department of bio­chemistry, and their collaborators.

Zein, the storage protein in corn kernels, belongs to a "highly complex, multigene family," Rubenstein says. Though abundant (making up as much as half of the protein content of seeds), the zein proteins have odd physical properties and consist of a family of 20 or more proteins, all having molecular weights of about 20,000.

Hence, Rubenstein, Messing, and their collaborators elected to cir­cumvent the worst difficulties of doing protein chemistry on zein by doing nucleic acid chemistry on its gene instead. That is, they obtained messenger RNA species from corn, cloned them in bacteria, made syn­thetic genes, and figured out the probable amino acid sequence of one type of zein from its gene sequence.

Whether or how much the struc­ture of this zein will typify the struc­ture of others in this family is not yet known, Rubenstein says. The protein contains many reiterations of partic­ular amino acid sequences at one end (the carboxy end) of the molecule, including a highly conserved 20-amino acid stretch that's repeated about eight times. "This is the first example of a repeated structure in a plant storage protein," Messing says. "We don't know if this will be general, the same in others. But this is a starting point."

It's too soon to know but not too soon to speculate about the impor­tance of such findings. A key fact to consider is that this zein protein contains no lysine. If that lack proves a steadfast and general rule for the entire family, renewed difficulties in genetically engineering these proteins for improved nutrition immediately become apparent. Because zein is believed to be a structural and storage protein without any catalytic activity,

its peculiar features, such as the many repeats, might be crucial for effi­ciently packaging it in seeds, Ruben­stein says. "Lysine may not be there [in zein] because of its positive charge which tends to collect water mole­cules—and that's maybe not good for seeds." Thus he speculates that tampering with zein's structure by [Hitting in lysine might not work, or at east might not be easy.

These early findings have a mar­velous way of prompting a near equal mix of pessimism and optimism in anyone looking for quick applications of genetic engineering in agriculture. Green's high-threonine variant in corn raises the possibility that a sim­ilar approach might well turn up a

high-lysine producer. But do a seed's biological requirements rule against it containing much lysine? The major storage proteins in seeds apparently lack lysine, and three-dimensional structural studies of those proteins eventually may explain why.

Meanwhile, the cornucopia is full of mixed guessings. It very well could be possible to put extra lysine, per­haps most likely as the free amino acid, into corn kernels. But its ab­sence under normal circumstances raises the equally plausible guess that corn as a biological entity prefers not having lysine there, quite possibly as the best way to ensure that seeds survive the hardships they were de­signed to endure. D

ACS celebrates Hildebri "Joel Hildebrand's birthday was Nov. 16, but so many people wanted to honor this wonderful couple that we had to wait our turn. Today is the turn of the American Chemical So­ciety."

That was how ACS president-elect Robert W. Parry opened the lun­cheon banquet celebrating Joel H. Hildebrand's 100th birthday held recently in Oakland, Calif. The lun­cheon, which drew nearly 600 well-wishers from around the world, capped a week of events honoring chemistry's most distinguished cen­tenarian, and Emily, his wife of 73 years (C&EN, Nov. 23, page 5).

It was a day of speeches lauding the many facets of Hildebrand's career and new honors for a man who has accumulated many through the years. It was also a day of reunion for many members of the extensive Hildebrand clan, with four generations repre­sented at the banquet.

Two of the important honors be­stowed at the banquet were the pre­sentation of $250,000 for endowment of the Joel H. Hildebrand Chair in Chemistry at the University of Cali­fornia, Berkeley, by Chevron Inc. and the presentation to Hildebrand of the first Joel H. Hildebrand Award in Theoretical & Experimental Chem­istry of Liquids, established by the Shell Companies Foundation as an annual ACS award.

The Hildebrand Chair in Chemis­try at Berkeley, unlike many such endowed chairs, will be rotated among assistant professors to help them in the early years of their re­search. In announcing the endow­ment of the chair, John R. Thomas, president of Chevron Research Co., said: "Prof. Hildebrand's scientific

id's 100th birthday contributions form the basis for many of the operations of the petroleum industry. The petroleum industry, and Chevron in particular, also is deeply indebted to Prof. Hildebrand for his unique contribution to edu­cation, as the well-being of our com­panies relies on a continued stream of well-trained and highly qualified professionals in all the science and engineering disciplines."

Berkeley chancellor Ira M. Hey-man, in accepting the endowment, said: "This chair is, in fact, very un­usual. Only one, or possibly two, chairs at Berkeley are named for faculty. I'm pleased for the recogni­tion this gives to a professor who represents the very best in the Berkeley faculty tradition—inspired teaching, vigorous and imaginative research, and spirited public ser­vice."

ι ζ

3

Shell Development's Papadopoulos pre­sents new ACS award to Hildebrand

Dec. 7, 1981 C&EN 33

Science

Michael N. Papadopoulos, a chemist at Shell Development Co., presented the new Hildebrand Award. "It is a great honor," he said, "to present this award to the out­standing scientist for whom it is named for his fundamental contri­butions to the understanding of in-termolecular forces, solubility, and the structure of liquids."

Also presented at the banquet were two works of art commissioned by ACS to commemorate the Hilde­brand centennial. Lawrence Berkeley Laboratory chemist Richard M. Lemmon, chairman of the Hilde­brand centennial committee, pointed out that "after a lot of fussing around with our artistic friends, we finally found two people and two kinds of art, both of which were eminently suitable for this purpose." However, the committee could not decide be­tween them, so they turned to Hil­debrand for help. Unlike his usually decisive self, Lemmon said, Hilde­brand would not decide for them. So both were commissioned, and Lem­mon presented them at the banquet to the University of California,

Berkeley. The first to be unveiled was a bronze bust of Hildebrand sculpted by Richard P. Murphy of Castro Valley, Calif. The second was a tap­estry by Alan Albert of Richmond, Calif., depicting aspects of Hilde­brand's life. Both works of art, ac­cording to C. Judson King, dean of the College of Chemistry, will be placed in the chemistry library in Hildebrand Hall on the Berkeley campus.

In the course of the banquet a number of speakers recalled aspects of Hildebrand's career. At the close of one of these talks, Berkeley chancel­lor Heyman read to the audience a number of his favorite Hildebrand quotes. In what he termed "a quota­tion especially meaningful to this audience," Heyman quoted Hilde­brand as saying: "What I have con­tributed to science has been small, but to have contributed even a minor part to the present imposing structure of science, and to have seen most of it under construction in my lifetime, has filled my days with exciting intellec­tual adventure."

Rudy Baum, San Francisco

Joel Hildebrand: still going strong

Emily and Joel Hildebrand

Call him not old, whose visionary brain

Holds o'er the past its undivided reign. For him in vain the envious seasons

roll Who bears eternal summer in his

soul. From Oliver Wendell Holmes, "The Autocrat of the Breakfast-Table"

The four lines are on a framed sampler hanging in Joel H. Hildebrand's living room near a large bookcase filled with the classics he reads aloud to his wife Emily in the evenings. The verse could not be more appropriate, for Hildebrand is the embodiment of the thought it ex­presses.

Hildebrand's latest paper, "A History of Solution Theory," leads off the most

recent Annual Reviews of Physical Chemistry. The edition is dedicated to the Hildebrand Centennial. When asked if he plans now to take a rest, he smiles and shakes his head. He is trying to de­cide, he says, whether he should revise "Regular and Related Solutions: the Solubility of Gases, Liquids, and Solids," a book he wrote in 1970 with J. M. Prausnitz and R. L. Scott, to incorporate recent findings on how methyl group substituents affect the solubility of cer­tain compounds.

"Everything I've done has been in­teresting," Hildebrand says. "I had a wonderful time," he says, recalling the early days of his career, "because a lot of things in chemistry were not right, and I was busy straightening them out." His most important contribution to chemis­try, he says, is his lifelong work with solutions. "Solubility is a central con­cept and to be able to predict how dif­ferent substances will dissolve finds application in all sorts of activities."

Hildebrand took teaching, as well as research, seriously. Science education in the U.S. has declined, he says, "largely because it has been taken over by professors of education." Also, Hil­debrand says, the best scientists should be writing textbooks and they aren't. "I was a pretty good scientist and I wrote texts," he points out with a grin.

Interest in protein chromatography grows The first international symposium devoted to high-performance liquid chromatography (HPLC) of proteins and peptides, held recently in Wash­ington, D.C, attracted hundreds of biochemically oriented researchers, many of whom had to be turned away because of lack of space. Organizers of the conference, which was .sponsored by Varian Associates, Palo Alto, Calif., expected 200 to attend. They were, in fact, inundated with more than twice that number.

Moreover, the attendees, compared to the usual crowd at such scientific meetings, seemed to be unusually attentive and absorbed in the tech­nical presentations, keynote lecturer Csaba Horvath of Yale University tells C&EN. According to Horvath, the papers presented at the sympo­sium make up roughly a third of all reports in the literature on HPLC of proteins.

This specialty is a relative new­comer that can boast an enormous potential for growth. It was born in the mid-1970's as a result of the de­velopment of rigid, microparticulate packing materials for HPLC columns. These column packings possess the properties of classical supports, but are rigid enough to permit high sol­vent flow rates under high pressures. Thus, they allow mixtures of large biological molecules to be separated with greater speed and higher reso­lution than has been possible with conventional gel matrices.

According to Purdue University biochemist Fred E. Régnier, one of the conference organizers, a great many researchers are reporting dra­matic successes in purification of bi­ological proteins and peptides with HPLC. The techniques they are using fall into three major classes: size ex­clusion chromatography, ion ex­change chromatography, and re­verse-phase chromatography. The third technique, in particular, has revolutionized peptide and protein chemistry, Régnier points out, since it has no equivalent in "classical" liquid chromatography.

Although the symposium was con­ceived by academic researchers, sci­entists in industry were represented amply. This is not surprising, Régnier says, since "biochemistry has come of age in industry." Recombinant DNA technology, for instance, is one of many areas in which industrial workers will be generating, separat­ing, and sequencing proteins. D

34 C&EN Dec. 7, 1981