Conversion of dihomo-gamma-linolenic acid to mono- and dihydroxy acids by potato lipoxygenase: evidence for the formation of 8,9-leukotriene A3

Evidence for the formation of a positional isomer of leukotriene (LT) C3 (8,9-LTC3) from dihomo-gamma-linolenic acid has been published (Hammarstr?m, S. J. Biol. Chem. 256, 7712-7714, 1981). This report describes the conversion of dihomo-gamma-linolenic acid to a postulated intermediate in former reaction, 8,9-LTA3, by purified lipoxygenase from potato tubers. 8(S)-Hydroperoxyeicosatrienoic acid (8(S)-HPETrE) was the most abundant dioxygenation product formed followed by 11-, 15-, and 12-HPETrEs (in decreasing order of abundance). In addition, 8(S),15(S)- plus 8(S), 15(R)-dihydroperoxyeicosatetraenoic acid (DiHPE-TrE) (EZE), and 8(S),15(S)- plus 8(S),15(R)-dihydroxy-eicosatetraenoic acid (DiHETrE) (EEE) were generated. Under anaerobic conditions only the latter two isomers of 8,15-DiHETrE (EEE) were obtained from 8-HPETrE. The results suggest that 8,9-LTA3 is synthesized by the sequential action of 8- and 11-lipoxygenase activities associated with the potato enzyme.     

The primary nucleotide sequence of U4 RNA

U4 RNA is one of the "capped" nuclear snRNAs recently found to be precipitable by anti-Sm antibodies as ribonucleoprotein particles. U4 RNA, along with other snRNAs, has been implicated in hnRNA processing, mRNA transport, or both (Lerner, M. R., Boyle, J., Mount, S., Wolin, S., and Steitz, J. A. (1980) Nature 283, 220-224). Since the proteins bound to different snRNAs appear to be the same, the functions of different snRNPs might be dependent on the RNA components. To help understand the function of U4 RNP, the nucleotide sequence of U4 RNA was determined. The sequence is (formula see text) In addition to the modified nucleotides in the "cap," U4 RNA contains Am at position 63 and m6A at position 98. It also exhibited A-C microheterogeneity at position 97.     

Rapid return of cyclo-oxygenase active platelets in dogs after a single oral dose of aspirin

A single dose of oral aspirin in human subjects inhibits the aggregation response of platelets to arachidonate and other agents for approximately one week after ingestion. In the present study we have evaluated the rate at which cyclo-oxygenase active platelets return to the circulation in humans and dogs and compared the response curves obtained to improvements in cyclo-oxygenase activity produced by the aspirin platelets. After a single dose of aspirin, dog platelet function was compromised for several days. Normal responses to arachidonate and other aggregating agents were restored six days after aspirin, and the pattern of recovery was the same for dogs and human subjects. However, cyclo-oxygenase active platelets returned to the circulation in dogs more rapidly than in humans and chemical competence was restored in both species well before correction of the defective response to aggregating agents. The delay of 1-3 days before return of significant numbers of cyclo-oxygenase active platelets most likely reflects acetylation of bone marrow megakaryocytes by the drug. More rapid return of chemically competent cells in dogs than humans probably relates to the more rapid turnover and shorter life span of canine platelets. The basis for the discrepancy in return of chemical integrity compared to functional activity after aspirin in vivo compared to simultaneous correction of chemistry and function when 10% normal platelets are added to aspirin platelets in vitro remains unresolved.     

Regulation by testosterone of the glucosamine-6-phosphate synthase activity in the male reproductive organs of rat

Accessory reproductive organs of male rat were found to contain high activities of glucosamine-6-phosphate synthase (glucosaminephosphate isomerase (glutamine-forming), EC 5.3.1.19). Castration caused drastic reduction (75%) in the enzyme activity of ventral prostate. Testosterone propionate administration restored the enzyme activity while cortisol and estradiol-17β did not cause any effect. Cycloheximide blocked the stimulation caused by testosterone.     

Inhibition of creatine kinase by iodoalkanes. Further appraisal of the essential nature of the reactive thiol group.

Creating kinase (ATP: creatine N-phosphotransferase) is completely inhibited by low molecular weight iodoalkanes in a pseudo first order reaction. Analysis of this and other data suggests that covalent modification per se is not a sufficient criterion to establish whether or not an enzyme group is essential for catalysis.