Thiocyanate ion formation in rapeseed meals.

Meal prepared from unheated rapeseed (Brassica napus cv. Zephyr) showed the presence of t,iocyanate ion, while meal from heated seed of the same cultivar did not show detectable amounts. Unheated seed meal on autolysis, and heated seed meal on incubation with thioglucosidase, yielded increased amounts of thiocyanate ion. Various commercial rapeseed meals showed the presence of t,iocyanate ion only after enzyme incubation. Low glucosinolate, cv. Bronowski, and higher glucosinolate, cv. Zephyr on enzymic incubation yielded comparable amounts of thiocyanate ion, suggesting that the precursor responsible in the two varieties was the same and present in similar quantities. No formation of thiocyanate ion was observed on incubation of sinigrin with thioglucosidase. Rats dosed with heated meal, containing intact glucosinolate, showed a slight increase of thiocyanate ion in the urine as compared with control rats dosed with water, while a relatively large increase followed dosing with sinigrin. Rats dosed with meal containing free thiocyanate ion excreted the ingested thiocyanate ion almost quantitatively.     

Rabbit liver transglutaminase: physical, chemical, and catalytic properties.

Transglutaminase (R-glutaminyl-peptide:amine alpha-glutamyl-yltransferase [EC 2.3.2.13]) has been purified to apparent homogeneity from extracts of rabbit liver. The enzyme is a single polypeptide chain of approximately 80 000 molecular weight containing one catalytic site per molecule. That the isolated enzyme is the rabbit counterpart of the well-characterized guinea pig liver transglutaminase is evidenced by the similarities in their amino acid compositions and in their enzymic activities toward several substrates, together with the fact that the isolated rabbit enzyme is immunologically distinct from both rabbit plasma and rabbit platelet blood coagulation factor XIII. A striking difference between the catalytic activities of the rabbit and guinea pig enzymes is the low activity of rabbit transglutaminase for hydroxylamine incorporation into benzyloxycarbonyl-L-glutaminylglycine, a reaction for which the guinea pig enzyme shows a high reactivity. This finding reveals the cause of error in an earlier report (Tyler, H.M., and Laki, K. (1967) Biochemistry 6, 3259) that rabbit liver contains little, if any, of the enzyme. Preparation of, and analytical data on, several glutamine-containing peptide derivatives used in this study are reported here.     

Induction of spherule formation in Physarum polycephalum by polyols

A method has been developed for inducing spherule formation (spherulation) in the myxomycete Physarum polycephalum by transferring the culture to synthetic medium containing 0.5 m mannitol or other polyols. This morphogenetic process occurred within 12 to 35 hr after the inducer was added. The mature spherules existed as distinct morphogenetic units, in contrast to the clusters of spherules formed during starvation. Ninety per cent of the spherules germinated by 24 hr in synthetic medium. The changes in the synthesis of ribonucleic acid (RNA), deoxyribonucleic acid (DNA), and protein during plasmodial growth, spherulation, and germination of spherules are described. When spherule formation was completed, RNA, protein, and DNA decreased, compared with the values at the beginning of the conversion. The incorporation of (3)H-uridine into trichloroacetic acid-insoluble material was different in each of these periods, and this incorporation was sensitive to actinomycin D. The amount of glycogen increased during growth, whereas it decreased during spherulation. (14)C-glucose could be taken up by the cells in the presence of the inducer, and mannitol could not replace glucose as a source of energy. The mode of action of mannitol and its mechanism of induction are discussed.     

Photoelectric signals from dried oriented purple membranes of Halobacterium halobium

In dried oriented samples of purple membrane isolated from Halobacterium halobium, the photoelectric activity decreases and the light adaptation vanishes when the water content of the sample is lowered. In the photocycle the first steps of the proton movement were accelerated with decreasing humidity, while the last steps of the photocycle could not be observed. From the analysis of the photoelectric signal we conclude that at low humidities the protons move forward in the L decay and return to their original place during M decay.