Plasmid-controlled mercury biotransformation by Clostridium cochlearium T-2.

A strain of Clostridium cochlearium having methylmercury-decomposing ability was isolated. The ability was cured by the treatment with acridine dye and recovered by the conjugation of the cured strain with the parent strain. The cured strain then showed the activity to methylate mercuric ion as previously reported (M. Yamada and K. Tonomura, J. Ferment. Technol. 50:159-166, 1971). These results and the agarose gel electrophoretic pattern of the deoxyribonucleic acids from the lysates indicate a possible role of plasmids in controlling the mercury biotransformation of the two opposite directions in a single bacterial strain: methylation in the absence of the plasmid and demethylation in the presence of it. A possible mechanism for mercury resistance involving hydrogen sulfide is discussed.     

Renin and Angiotensin-Converting Enzyme in Human Neuroblastoma Tissue

High activity of renin was demonstrated in human neuroblastoma tissue. This activity was inhibited by specific antibody raised against human renal renin, indicating that it was not due to the nonspecific action of proteases. The specific activity of renin was 122.8 ng of angiotensin I generated mg of protein-1 h-1. It shared some biochemical features with well-known kidney renin, such as molecular weight, optimum pH, the presence of trypsin-activatable inactive renin, and glycoprotein nature. Furthermore, angiotensin-converting enzyme (ACE) activity (2.64 nmol mg of protein-1 min-1) was found in the tissue. This activity was inhibited by captopril, a specific ACE inhibitor, or by omission of chloride ion. These results suggest that true renin in addition to ACE exists in human neuroblastoma tissue.