The direct detection, using the polymerase chain reaction (PCR), of Listeria monocytogenes added to cows' milk was inhibited at some milk concentrations. This inhibitor was moderately heat‐stable. Inhibition could be prevented by the addition of Bovine Serum Albumin (BSA) or proteinase inhibitors to the PCR and the evidence suggests that the inhibitor was plasmin.

SUMMARYSynechocystis PCC 6803 and Anabaena variabilis ATCC 29413 showed a high degree of tolerance to the herbicide glyphosate, applied as the free acid, the monoisopropylamine sait or the commercial formulation (Roundup''). Differential toxicity between herbicide formulations was observed (Roundup > isopropylamine salt > free acid) and correlated with their rates of uptake. There was no evidence of glyphosate degradation. Shikimate accumulation, together with partial alleviation of inhibition by aromatic amino acids, suggests that the target site for glyphosate is in the pathway of aromatic amino acid biosynthesis.

5-Enolpyruvylshikimate 3-phosphate (EPSP) synthase (3-phosphoshikimate 1-carboxyvinyltransferase; EC 2.5.1.9) from the glyphosate-tolerant cyanobacterium Anabaena variabilis (ATCC 29413) was purified to homogeneity. The enzyme had a similar relative molecular mass to other EPSP synthases and showed similar kinetic properties except for a greatly elevated K i for the herbicide glyphosate (approximately ten times higher than that of enzymes from other sources). With whole cells, the monoisopropylamine salt of glyphosate was more toxic than the free acid but the effects of the free acid and monoisopropylamine salt on purified EPSP synthase were identical.