The salt-soluble proteins from rapeseed (Brassica napus L.), variety Nugget, have been extracted with 0.01 M sodium pyrophosphate (pH 7.0) and with 10% sodium chloride, and subsequently separated into a number of components. There are two major proteins in the pyrophosphate salt extract, one is neutral (the 12 S protein) and the other is basic (the 1.7 S protein). They constitute 30% of the nitrogen in the extract. There are nine other minor components in this extract. The 10% sodium chloride extract contains a water-insoluble protein (the 12 S protein) which constitutes 21% of the nitrogen in the extract and appears to be similar in properties to the 12 S protein in the pyrophosphate salt extract. This protein, upon sedimentation analysis in 6 M urea solution and in 0.1 M glycine–HCl buffer (pH 2.2), appeared to be an aggregate of units of smaller molecular weight.

Phenolic compounds in Commander, Majak, and Valley sunflowers varied between 3.0 and 3.5 g of chlorogenic acid per 100 g of flour. Under neutral and alkaline conditions, sunflower protein solutions develop dark green and brown colors because of bonding with oxidation products of polyphenolic compounds, especially chlorogenic acid. Therefore, a reducing agent was utilized in the present study to inhibit the formation of covalent bonds but 30% of the chlorogenic acid was nondialyzable and remained bound to the flour constituents. About one-half of the phenolic constituents were extracted with the soluble sunflower proteins by neutral salt solutions and about onethird o:: this fraction was also nondialyzable.Fractionation of the neutral salt extracts revealed that all of the soluble chlorogenic acid was associated with the low molecular weight components (mol wt <5000) in the third fraction on Sephadex G-25 and fraction V in Sephadex G-200 chromatography. The elution behavior on Sephadex gels, the low nitrogen contents, and the low amino acid recoveries demonstrated that these fractions were polypeptides and oligonucleotides. Rechromatography of fraction V on Sephadex G-200 in the presence of a strong hydrogen bonding agent, 7 M urea, revealed that 68% of the salt-soluble polypeptides were hydrogen bonded and about 32% were apparently covalent bonded to chlorogenic acid in Commander sunflower.Sunflower is one of the fastest developing oilseed crops and ranks second in importance as a world source of vegetable oil. The fibrous by-product of oil extraction is uti-

Amino acid compositions of casein, egg white, beef, soy isolate, rapeseed concentrate, pea flour and wheat flour were studied by seven collaborating laboratories. Samples were hydrolyzed with 6N HCl, performic acid + 6N HCl, and (with one exception) 4.2N NaOH. Amino acids were then determined by ion-exchange cbromatography using automatic analyzers. One laboratory, however, determined tryptophan by treatment with p-dirnethylaminobenzaldehyde. The calorimetric determination of tryptophan was comparable to the tryptophan values determined by ion-exchange chromatography. Interlaboratory variation of tryptophan (coefficients of variation, CV, up to 24%), cystine and methionine (CV up to 17%), was greater than that of most other amino acids (CV up to 10%). Intralaboratory variation for all amino acids was less than 5%.

Two African species of Aspilia (Asteraceae), which are used medicinally by man and which are eaten by wild chimpanzees in an unusual manner, were found to contain the potent antibiotic thiarubrine A as a major leaf phytochemical. Its presence in leaf material strengthens the view that the feeding behavior of wild chimpanzees is related to special physiological or pharmacological effects on the animals.